CAZyme Information: KIW97339.1

Basic Information

• Species: Cladophialophora bantiana
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora bantiana
• CAZyme ID: KIW97339.1
• CAZy Family: GT22
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
646	KN846982|CGC10	72279.80	6.6728

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CbantianaCBS173.52	12817	1442370	55	12762

• Gene Location: location=KN846982:2299519-2301459(+)

Full Sequence      

MERTNSRRRKVGVSKVGDSRNTIPSAPPALARTARDEFSAPIEAPSWDFKTAGYFSGMLM
FLLLSTLLLGQFGSDSSLLRAVKNILWRSDLRNHEQPLGDIAVKLHPDAHVRRPPTTLTF
NWEITKGFRYPDGVRKEVYLINGQFPGETIEARSGDRIVVNVTNLLIDEGLAIHWHGLRM
KGANDMDGAVGLTQDPIPRGQSYLYNFTIGEEESGTFWYHGHEKTQRDDGLYGGLVVHRP
LHQLNEKETYHYDEEILLLIGDWYHRPSTEVLRWYMNSRSFGNEPVPDSLVVNGKGDFSC
DMAVPARPVDCIPSIERTDLPLLRVESIKRYRLRLVNTGSLTGFSIKMDNASLSPFQVDA
GHEITKIGARGVGIVYPGERVDAILQTGLSDTQCHLKIEMDDENFKYPNPALNPLQTFPV
KIGSDSASKRQVLRPELKYYNLQAALPNHSSPIAWSDEPLKFVLYTTTLKLARHHNIPMG
FINHTSWSPQSPPLISLAREQYDQNQLSPHIPFSEDDGAAIAGDAGGWVEVVINNLDDGG
HPFHLHGHSFYVVSVFPPPIPWSSEKPSFTAGGSAMYNYDPFASPPSESPAGPYNLVNPV
MKDTVFVPQRGYVVIRFRADNKGTWMMHCHVGWHLGSGMAMSWEVS

Enzyme Prediction     

No EC number prediction in KIW97339.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	134	640	8.6e-89	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	4.08e-74	120	644	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	5.43e-67	120	641	26	542	L-ascorbate oxidase
215324	PLN02604	2.11e-61	108	644	21	545	oxidoreductase
274556	laccase	9.86e-57	134	645	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.
259869	CuRO_1_LCC_like	8.99e-53	119	238	2	120	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI22443.1|AA1	4.28e-175	97	645	80	606
UPK99837.1|AA1	9.65e-173	99	645	80	600
QKD61545.1|AA1	4.78e-171	101	645	75	596
AVI02163.1|AA1	1.35e-170	101	645	75	596
UKZ83242.1|AA1	2.34e-170	91	645	76	610

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	3.20e-54	120	641	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	5.00e-53	131	646	81	543	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.31e-52	131	646	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	2.07e-52	117	641	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]
5Z1X_A	1.30e-46	131	641	17	461	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	4.63e-63	105	638	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|Q55P57|LAC1_CRYNB	1.50e-58	105	638	49	553	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|P14133|ASO_CUCSA	1.02e-57	115	641	36	555	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|J5JH35|OPS5_BEAB2	7.54e-57	99	641	55	547	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q40588|ASO_TOBAC	1.53e-55	117	641	30	546	L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999900	0.000117

TMHMM  Annotations     

Start	End
52	74