CAZyme Information: CAP96595:RNA-p1

Basic Information

• Species: Penicillium rubens
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicillium; Penicillium rubens
• CAZyme ID: CAP96595:RNA-p1
• CAZy Family: GH76
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
585	Pc00c21|CGC5	65155.97	4.9802

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PrubensWisconsin54-1255	14021	500485	1464	12557

• Gene Location: location=Pc00c21:4004748-4006560(-)

Full Sequence      

MCRILPTLFCLVVGLATATATQGLASRHDNSFQPDHILRVTAQSYSQACMERYSVLVNGS
SPGPELRLQEGRVSWIRVYNDMEGLNTTMHWHGLSAFTAPFSDGAPMASQWPIAPGHFFD
YEVRPEIGYAGTYFYHSHVGFQAVTAGGALIVESAQPSPYEYDEERIIALTDFFAKTDEE
IEDGLSSANFTWSGETGAVLVNGQGRLATDASGSCKLAAISVEPGKTYRLRFVGATALSF
VSLAIESHDLFEIIEADGHYTKPVKTSYLQISSGQRYSVLLKAKTEAELQEARSRQFYFQ
LTTLGRPTVLTTFAVLEYPSPFATDLATVPVTPPLPVADIIHGWMDYALEPYYPDPNFPT
AEEVTRRIIINVHQNVSSHVIWLQSGYDWMETFPMSPYLVDVYNGKLDLDDSYERAIASG
YGFDNQTRLFPAKIDEVLEIVWQNQGAVNTGNVENHPFHGHGRHFYDVGGGDGLYKPEEN
EKRLNGTHPVTRDTSVLYAYRSETEALAPSGWRAWRIRVTNAGVWMMHCHFLQHMVMGMQ
TVFAFGDEADIRAQSGPVDEGYLTYGGSAYGNATHYPLVQHFYDV

Enzyme Prediction     

No EC number prediction in CAP96595:RNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	47	540	2.7e-91	0.9832402234636871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
132431	ascorbOXfungal	0.0	27	552	2	538	L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized.
274555	ascorbase	8.34e-95	49	546	17	524	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.
259962	CuRO_3_AAO_like_2	1.11e-85	363	546	1	188	The third cupredoxin domain of Ascorbate oxidase homologs. This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (MCO) family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds 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 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.
215324	PLN02604	3.09e-81	46	548	37	549	oxidoreductase
177843	PLN02191	7.26e-80	11	546	10	547	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW38925.1|AA1	0.0	11	584	17	588
QMW26845.1|AA1	0.0	11	584	17	588
QRD81157.1|AA1	0.0	11	584	18	589
UDD54641.1|AA1	0.0	11	584	17	588
BCS19632.1|AA1	6.06e-303	11	584	8	578

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	8.50e-61	49	548	19	526	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]
6KLG_A	1.07e-43	40	543	10	528	Crystal Structure of the Zea Mays laccase 3 [Zea mays],6KLI_A Crystal Structure of the Zea Mays laccase 3 complexed with sinapyl [Zea mays],6KLJ_A Crystal Structure of the Zea Mays laccase 3 complexed with coniferyl [Zea mays]
1HFU_A	7.66e-34	38	559	9	482	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	7.75e-34	38	559	9	482	Chain A, Laccase [Coprinopsis cinerea]
1ZPU_A	2.24e-32	55	542	25	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QFD0|LMCO1_MYCTT	3.07e-172	28	584	25	632	Laccase-like multicopper oxidase 1 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=LMCO1 PE=1 SV=1
sp|I1RF64|AURL2_GIBZE	9.03e-165	28	584	22	598	Multicopper oxidase aurL2 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=aurL2 PE=2 SV=1
sp|Q0D1P3|TERE_ASPTN	9.72e-130	89	584	1	528	Multicopper oxidase terE OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=terE PE=1 SV=1
sp|P14133|ASO_CUCSA	1.70e-62	45	546	50	560	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|M4DUF2|ASO_BRARP	6.29e-61	49	546	36	543	L-ascorbate oxidase OS=Brassica rapa subsp. pekinensis OX=51351 GN=AO PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000222	0.999777	CS pos: 20-21. Pr: 0.8456

TMHMM  Annotations     

There is no transmembrane helices in CAP96595:RNA-p1.