CAZyme Information: PV07_07155-t44_1-p1

Basic Information

• Species: Cladophialophora immunda
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora immunda
• CAZyme ID: PV07_07155-t44_1-p1
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
639		71860.93	6.0378

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CimmundaCBS83496	12879	N/A	49	12830

• Gene Location: location=KN847043.1:2202008-2203927(+)

Full Sequence      

MERTNSRRRKAGGVKPDDPHDAVASAPTVSTNTAKERSPTTLEAPSREFKTARLFSGLLL
FLLVSALLLDQLGGGSWLLKRIQNPLREHGMQHQTQTAGDIATKLHPDAHIGRPPTTLTF
DWEVTKSYRYPDGVRKEVYLINGQFPGETIEARSGDRIMVNVSNLLRDEGLAIHWHGLRM
EGANDMDGAVGLTQDPIPSGASYLYNYTIGEEEFGTFWYHGHEKTQRDDGLYGGLVIHRP
LTQLSEKDTYHYDEEILLLVGDWYHRPSTEVLRWYMNSRSFGNEPVPDSLVINGKGRFSC
DMAVPARPLDCIPSNERGDLPVLHIENDKRYRLRLVNTGSLTGFSMRMDNASFSPFQVDG
GHDITMTEVQGMGILYPGERVDVILQTGVSDSHRYLEIEMDDENFKYPNPALDPLQKFPV
ETESESTQQRQVLQPELQYYNLQAALPSHSLPIAWADESLKFVIYTTTLKLARHHNIPMG
FINHTSWSPQSPPLLSLARERYDSNQLSPHIPLAKDGAAGWVEIVINNLDDGGHPFHLHG
YSFYVVSVFPPPIPWSSDKPPFTAGGTGMYNYDPFSSLPSESPAGLYNLENPVMKDTVFV
PQRGYVVIRFRADNKGTWMMHCHVGWHLGSGMAMSWEIS

Enzyme Prediction     

No EC number prediction in PV07_07155-t44_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	134	633	1.9e-90	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.15e-76	120	637	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	1.80e-67	122	634	28	542	L-ascorbate oxidase
215324	PLN02604	1.47e-64	120	637	27	545	oxidoreductase
274556	laccase	4.52e-56	134	636	20	517	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	2.82e-53	462	634	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	6.75e-175	101	632	85	600
UPK99837.1|AA1	1.90e-173	17	638	5	600
QKD61545.1|AA1	2.75e-168	101	638	75	596
QPC62885.1|AA1	3.00e-168	87	637	69	599
AVI02163.1|AA1	7.77e-168	101	638	75	596

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	2.86e-54	120	634	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	1.95e-53	117	634	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	2.85e-51	115	634	63	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	7.42e-51	115	634	63	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]
5EHF_A	1.81e-47	121	634	7	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	2.91e-63	88	631	32	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|J5JH35|OPS5_BEAB2	4.00e-63	114	634	68	547	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	3.08e-62	81	631	25	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	6.91e-59	91	631	35	553	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|P24792|ASO_CUCMA	6.61e-54	120	634	36	549	L-ascorbate oxidase OS=Cucurbita maxima OX=3661 GN=AAO PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999910	0.000095

TMHMM  Annotations     

Start	End
57	79