CAZyme Information: PABG_05667-t30_1-p1

Basic Information

• Species: Paracoccidioides brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides brasiliensis
• CAZyme ID: PABG_05667-t30_1-p1
• CAZy Family: GH76
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
655		72939.65	8.0747

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PbrasiliensisPb03	8548	482561	121	8427

• Gene Location: location=KN305539:970626-973182(+)

Full Sequence      

MERPSSRRRIRGARNSQECRRESPGSGEGKPSQGTVHWSNRHLAVVVISVISLVALFRVL
EGSNIPGYLPGLALKEHVLDVSLHPATEELHPEDHIYRRATTIHLNWTVTAGDRHPDGVR
KSVYLINGRFPGPTIEARSGDRLIINVKNGLADEGVSVHWHGLHMKDGNRMDGTTGVTQC
AIAPQESFPYDFTISDSQSGTYWYHAHSGLQRADGLYGGLVIHRPAPRGVRGVQLRHPES
DILRYNYQKEILLLVGDWYHRRAHDVLEWYMRAGSYGNEPVPDSLVINGAGHFNCAQAVP
ARPVDCLEDGHPVPYLIIDPTQSYRVRLVNTGSLAGISLGVAQGYLDVLHLDGGLDVQEL
RRPKTSNPQSIGILYPGQRVDFILRHHRNAPAKSSLTVELDPECFKYSNPALSSLQSFPI
YSTISKSIKQTSLPQPLTLPAKNHIDLTQVSSTPALLSGLPPEADQTYVVYTKISKMSKN
HNVPLGYFNHTSWRPQSTPRYPLIALDPHDWDKNQLAISTGSKLVWVDLVINNLDEGAHP
FHLHGHDFFVLTLHAATQGWGSYNPFDPHPRHQQFRPSSKDLEKAVLRDTVQIPQRGHAV
LRFRADNPGVWLLHCHILWHLAAGMAMVIDVMNGFNVGEKPGIAGGENIAMCQYF

Enzyme Prediction     

No EC number prediction in PABG_05667-t30_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	119	626	1e-89	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.21e-72	104	628	3	520	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	1.07e-71	100	646	21	560	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	1.56e-63	468	631	1	166	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.
274556	laccase	1.15e-61	119	634	20	522	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	2.87e-60	100	630	22	545	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS75251.1|AA1	1.39e-274	171	654	1	482
QKX62088.1|AA1	1.24e-212	90	649	97	671
QGA16928.1|AA1	1.34e-210	90	630	108	668
QSS54105.1|AA1	5.20e-208	271	654	1	382
UPX44859.1|AA1	6.58e-207	90	646	80	644

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.15e-57	104	628	5	520	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	2.13e-57	106	653	6	501	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	3.04e-53	116	627	81	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	7.94e-53	116	627	81	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]
5LM8_A	6.06e-48	117	636	38	510	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RMG9|FET3_GIBZE	2.06e-65	99	625	21	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	3.97e-65	100	625	20	489	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|E9R598|FETC_ASPFU	7.88e-63	100	626	20	487	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|Q6CII3|FET3_KLULA	5.93e-61	99	629	24	503	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|Q8LPL3|ASO_ARATH	5.09e-60	100	628	21	540	L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999916	0.000097

TMHMM  Annotations     

Start	End
43	60