CAZyme Information: ETI23479.1

Basic Information

• Species: Cladophialophora carrionii
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora carrionii
• CAZyme ID: ETI23479.1
• CAZy Family: GH16
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
638	KB822705|CGC15	71259.50	5.8117

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CcarrioniiCBS160.54	10428	1279043	55	10373

• Gene Location: location=KB822705:1711042-1712958(-)

Full Sequence      

MERTNSRRRKAKVSEANSPVDASVMVELTPPKDEVSTACKAPSWLPNTACWVVVLLIFVL
TAAFLLAYPEGLPLINEQKPTTIQIHGDEQYHGGVGIVLHPESHVSRPPATLCFDWRVTK
AFRSPDGVRKEVYVINDQFPGPTIEARSGDRIIVNVTNLLHKEGLAIHWHGLRMKDANDM
DGAVGLTQAPIQTGETFLYNFTIGHDEFGTFWYHGHEKTQRDDGLYGGFIIHRPVEQSDE
KEVYDYAQEVLLLIGDWYHRPSTDVLRWYMNSRSFGNEPVPDSLLINDHGNFDCDMAVPA
RPLQCTPPAARDELPSLRFDRGHRYRLRLVNTGSLTGFSLKVDAASLFPFQVDGGNSIDM
AEAQSIGIVYPGERVDAILLLESNYRRRELTIEMDDENFKYPNPALTPMQTFPVTSSPSD
GDATQPVPPMLEYYNLQAAVSGSGSLTGMTEEPLKFVVYTTTMKLAKHHNIPMGFINHTS
WSPQAEPLISLPRSQYDRNQLSPHVGLCQTENETAACNEWVEVVINNLDDGGHPFHLHGY
SFYVVSVFPPPIPWSSEKPPFTPGGSGMYNYNPFTTTSAVSPAGPYNLANPVVKDTVFVP
QRGYAVIRFRADNKGIWMMHCHVGWHLGSGMAMSWDVS

Enzyme Prediction     

No EC number prediction in ETI23479.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	128	632	1e-89	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.11e-72	114	631	4	517	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	9.30e-66	116	633	28	542	L-ascorbate oxidase
274556	laccase	5.07e-56	128	637	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.
215324	PLN02604	7.64e-56	114	631	27	540	oxidoreductase
259977	CuRO_3_MCO_like_4	1.03e-53	456	633	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
UPK99837.1|AA1	4.05e-175	93	637	80	600
QKD61545.1|AA1	4.41e-175	21	633	20	592
AVI02163.1|AA1	1.25e-174	21	633	20	592
UNI22443.1|AA1	1.52e-170	95	632	85	601
QRD88142.1|AA1	6.45e-170	29	637	15	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.11e-55	114	633	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]
1ZPU_A	2.52e-52	111	633	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]
3V9E_A	1.08e-51	124	633	80	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.81e-51	124	633	80	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]
6H5Y_A	1.51e-45	115	633	7	462	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	3.67e-60	99	630	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|J9VQZ4|LAC2_CRYNH	1.04e-58	98	630	48	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
sp|Q55P57|LAC1_CRYNB	1.30e-58	99	630	49	553	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|I1RMG9|FET3_GIBZE	3.16e-57	110	631	23	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	5.44e-55	110	632	21	490	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999883	0.000133

TMHMM  Annotations     

Start	End
49	68