CAZyme Information: EXJ72401.1

Basic Information

• Species: Cladophialophora psammophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora psammophila
• CAZyme ID: EXJ72401.1
• CAZy Family: GH55
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
645		72025.35	6.6045

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CpsammophilaCBS110553	13421	1182543	0	13421

• Gene Location: location=AMGX01000006:1585800-1587737(+)

Full Sequence      

MERTNSRRRKAGVPKIDDSHNAIPSTPPPLARTARDQFTAPIEAPSWHFKTAGYFSGMLM
FLLLSTLLLSQFGSDSSLLRAIKNTLWRSDLQNQEQPVGDIAVKLHPDAHVGRPPTTLTF
NWEITKGFRYPDGVRKEVYLINGQFPGETIEARSGDRIVVNVTNLLIGEGLAIHWHGLRM
KGANDMDGAVGLTQDPIPRGQSYLYNFTIGQEESGTFWYHGHEKTQRDDGLYGGLVVHRP
LHQLNEKETYHYDEEILLLIGDWYHRPSTEVLRWYMNSRSFGNEPVPDSLVVNGKGDFSC
DMAVPARPVDCIPSNERTDLPLLRVESGTRYRLRLVNTGSLTGFSIKMNNGSLSPFQVDA
GHEITKIGAQGVGIVYPGERMDAILQTGVSDTQCHLEIEMDDENFKYPNPALNPLQTFPV
KIGTNSAYERQVRQPELKYYNLQAALPNSSSPIAWSDAPLKFVLYTTTLKLARHHNIPMG
FINHTSWSPQSPPLISLAREQYDQNQLSPHIPFAKDGDAIAGDAGGWVEVVINNLDDGGH
PFHLHGHSFYVVSVFPPPIPWSSEKPPFTAGGSAMYNYDPFASPPSESPAGPYNLVNPVM
KDTVFIPQRGYVVIRFRADNKGTWMMHCHVGWHLGSGMAMSWEVS

Enzyme Prediction     

No EC number prediction in EXJ72401.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	134	639	3.8e-89	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.91e-77	120	643	4	522	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	1.76e-68	120	640	26	542	L-ascorbate oxidase
215324	PLN02604	6.17e-64	120	643	27	545	oxidoreductase
274556	laccase	1.83e-58	134	644	20	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.
259977	CuRO_3_MCO_like_4	6.72e-54	462	640	1	162	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI22443.1|AA1	1.88e-173	97	644	80	606
UPK99837.1|AA1	3.30e-173	68	644	56	600
QKD61545.1|AA1	2.69e-167	91	644	63	596
QMW37919.1|AA1	4.83e-167	102	644	77	598
QRD88142.1|AA1	5.92e-167	58	644	46	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	2.39e-55	120	640	6	519	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	1.99e-54	131	645	81	543	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	5.22e-54	131	645	81	543	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]
1ZPU_A	1.02e-51	117	640	2	475	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]
5EHF_A	5.11e-47	131	640	17	463	Laccase from Antrodiella faginea [Antrodiella faginea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	4.44e-62	105	637	49	553	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|P14133|ASO_CUCSA	1.39e-57	115	640	36	555	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	1.41e-57	105	637	49	553	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J5JH35|OPS5_BEAB2	1.95e-56	131	640	87	547	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	2.77e-55	105	637	49	553	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999946	0.000068

TMHMM  Annotations     

Start	End
52	74