CAZyme Information: RO3G_15489-t26_1-p1

Basic Information

• Species: Rhizopus delemar
• Lineage: Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus delemar
• CAZyme ID: RO3G_15489-t26_1-p1
• CAZy Family: GT48
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
697		80404.58	8.8666

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RdelemarRA99-880	17703	246409	244	17459

• Gene Location: location=CH476747:548040-550200(+)

Full Sequence      

MYIKSFIAIGLLITLSQAALQRFEFNIDYRAVNPDCHKESFNVPAINGQFPGPTIYATEG
DEIEVLVRNQLGNANTSIHYHGIRQIGSTESDGVPGVTQEPIRPGRSFRHRFLITQAGTY
FYHAHVGLQDDSVQGAFIVYESPKADPRRHHRLEKRCTHQKRTCQSRTRALLEAGPYTYK
KDLILQLSEWWHDELSSRQDYYMGSAFKYDHGADSILFNGRTIHDPLVTDGTRCLGYTTL
DVEPNSVYRLRVIGGNTFRTLALGIKNHNMTLIEVDGELIHPYQTSFLEVTPGQRFSVLL
YTGNYQPGTTFAIGTSYLWRQRGRGITENGFAYIRYVERHPDTNHSHLFKSLSKWYEPKK
SKGRWGNDDQTRGRTVGDGSDHARGSRADNAAEHNGRKWNGEGTDHRERKTWDDKTRSDA
DVKKKSGLKKRQGVWNDKGDHSWPRNRDHHHLDQGTNKTVGHSYHFGGHQQHDDNAYEDL
PTFPRMDQPDWIWHHLTPLALRDPILDATKVRTIRLHTSLRQMSDNTTRYFVNNRTNPIR
PVPALYHFSHFHKRATDEYDDDFYTDLHTYRIEYNEIIDLVFQNTKSKGGGCMLHPWHTH
GHSHYVIASGSGDYIHDLHKNIRNFKTPLYKDTSVAYPSYSNDQSNGCGWTKVRFKADNP
GFWAVHCHITTHMMQGKMIVLEEAPNLISKHRLYNHE

Enzyme Prediction     

No EC number prediction in RO3G_15489-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	42	676	8.9e-87	0.9664804469273743

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.04e-76	22	690	3	530	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	4.10e-70	7	690	10	553	L-ascorbate oxidase
215324	PLN02604	2.43e-68	5	690	9	553	oxidoreductase
274556	laccase	5.88e-52	18	681	1	518	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.
259868	CuRO_2_LCC_like	5.43e-51	184	336	2	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) 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 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 2 of 3-domain MCOs has lost the ability to bind copper.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS06551.1|AA1	3.25e-160	20	694	25	651
CDS12532.1|AA1	5.62e-123	23	688	30	573
CDS06185.1|AA1	9.55e-119	23	689	18	571
CDS07261.1|AA1	2.61e-86	16	655	18	519
CAG1837461.1|AA1	1.73e-58	15	690	31	561

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	7.59e-45	20	690	3	530	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	2.56e-36	28	685	12	481	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]
6KLG_A	8.45e-29	23	676	6	523	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]
3SQR_A	3.34e-28	21	300	68	315	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]
3V9E_A	3.34e-28	21	300	68	315	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|M4DUF2|ASO_BRARP	3.36e-52	7	690	7	549	L-ascorbate oxidase OS=Brassica rapa subsp. pekinensis OX=51351 GN=AO PE=2 SV=1
sp|Q8LPL3|ASO_ARATH	3.27e-51	16	690	19	550	L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1
sp|P14133|ASO_CUCSA	5.76e-48	7	688	22	564	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|Q40588|ASO_TOBAC	2.40e-47	18	690	28	557	L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1
sp|P37064|ASO_CUCPM	3.90e-44	20	690	3	530	L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000243	0.999717	CS pos: 18-19. Pr: 0.9821

TMHMM  Annotations     

There is no transmembrane helices in RO3G_15489-t26_1-p1.