CAZyme Information: ASPBRDRAFT_171585-t33_1-p1

Basic Information

• Species: Aspergillus brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis
• CAZyme ID: ASPBRDRAFT_171585-t33_1-p1
• CAZy Family: GH114
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
618		68787.73	6.6831

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AbrasiliensisCBS101740	13263	767769	274	12989

• Gene Location: location=KV878681:982855-985087(+)

Full Sequence      

MLSAMRDVDLSISPLSKMKKRTNILSDAQQSPSLPLRRLPWSIVLYPAITCGLILLLFLT
QISQSGPLQGLIPFGDSNSQIHSITHNPDTSRPLIKLHPENHIYRDPTTQHLDWVVTADH
LRPDGVLKRVYLVNGLFPGPTVEARSGDCLIVNVTNALDDEPISVHWHGIHIENAMDGAV
GVTQRPIPPGSTFTYDFTIPADQSGTFWYHAHSGLIRADGLYGGLIVHKPSPKATVRGLL
ARADGRELGSYDKDILLLVGDWYHRSADQVYSWYMRAGSFGNEPVPDSLLINGMNVSYLD
AKSDAKYRVRVVNTGSVAGFTLGLQNRDFTLIQVDSIDVEQQDTDSAGVLYPGQRMDIIL
HPSHTDSSSSLTIDLNKECFRYPNPALASTQTFEIARSPDNSFPTISPLNSTISLSEVAT
KRPLLSGLPEKAHQTHVVYTKIEKLSINHNVPYGFFNRTSWKPQLDTPVIDLPRDQWDIN
QLVISTGSTVSRQSSSSDQNRDLWIDLVVNNLDDSGHPFHLHGHHFYILRTYQAPIGWGA
YNPFTDAYPPGLAAQHASSSTPDIPYDLSRAQLRDTVYIPSRGHAVLRFRADNPGIWLFH
CHIIWHQASGMAMLMQIE

Enzyme Prediction     

No EC number prediction in ASPBRDRAFT_171585-t33_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	126	612	1.8e-91	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	7.30e-60	114	612	38	443	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
274555	ascorbase	8.17e-60	109	611	1	517	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.
259977	CuRO_3_MCO_like_4	1.24e-57	437	613	2	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.
177843	PLN02191	3.78e-57	114	614	28	543	L-ascorbate oxidase
259869	CuRO_1_LCC_like	2.48e-52	110	228	1	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
CAK44017.1|AA1	0.0	29	617	2	586
BCS06095.1|AA1	2.21e-277	176	618	1	460
BCR93452.1|AA1	2.21e-277	176	618	1	460
QMW37919.1|AA1	3.85e-254	31	617	8	598
QRD88142.1|AA1	5.74e-253	31	617	25	615

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	2.15e-58	109	615	2	477	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	4.34e-53	121	613	79	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.14e-52	121	613	79	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	6.30e-52	124	612	38	499	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.41e-52	124	612	39	500	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6CII3|FET3_KLULA	3.04e-64	109	615	27	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|I1RMG9|FET3_GIBZE	3.51e-63	109	611	24	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|P43561|FET5_YEAST	2.50e-62	109	612	20	508	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1
sp|K7NCS2|FETC_EPIFE	1.28e-61	113	612	26	490	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|P78591|FET3_CANAX	2.49e-60	123	615	37	496	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999954	0.000052

TMHMM  Annotations     

Start	End
41	63