CAZyme Information: ATEG_08458-t26_1-p1

Basic Information

• Species: Aspergillus terreus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus
• CAZyme ID: ATEG_08458-t26_1-p1
• CAZy Family: GT1
• CAZyme Description: predicted protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
605		67579.40	4.4846

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AterreusNIH2624	10551	341663	150	10401

• Gene Location: location=CH476605:1308931-1311091(+)

Full Sequence      

MPSLKDWVVAGLVPMTIASSTSRLPSNCTNGPSSRRCWQDGFDIWSDYTDPKVAPPGKLV
EYDLTVTQVTISPDGYERLGTVFNGQYPGPLIEADWGDTLRITVHNNLTNGNGTAVHWHG
IRLFETNWIDGVPGVTQCPIPPGESQVYEFRATQYGTSWYHSHFSLQYSNGLYGPLVIHG
PSSSDWDVDLGPWTLTDWYHEDAFTLNWISLAGQLAPIPVSTLLNGKGTYDCDPGLDPAC
TGKQEYFETTFQQGTKYKMAIVNTATLLTYTFWIDGHNFTVIEADFVPVEPYSTNVLNVG
MGQRYEIVVEANADRTQGSSFWIHAHYCDIPDVIPNNKVGIIRYDESDTSEPATPPLSEQ
HRDFGCSDPSLGDLVPVVKKTVGPRVNQIGPHDYLTIGEQGKIPTPWEKDPRVHLWTIKN
TAMYVDWQTPSLEKLTADHDEEFPPETVPVTLDFDTGEWVYFLLTSNYSLEDVVTPRNLT
PSVHPIHLHGHDFAILAQGKGPFTPDIAPQLDNPPRRDVVDVDIGGYAWIAFEVDNPGAW
LLHCHLQYHASEGMALQYIEQPSKIKPLIENAGVLNDFGNRCASWKRYYNAVDIPNDRPQ
DDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	52	358	6.9e-124	0.9615384615384616

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.29e-74	60	568	8	531	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	2.73e-73	59	572	23	558	L-ascorbate oxidase
215324	PLN02604	4.77e-72	72	573	37	562	oxidoreductase
259923	CuRO_1_MaLCC_like	1.27e-70	57	179	1	122	The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. 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.
259947	CuRO_2_MaLCC_like	5.81e-66	190	358	1	167	The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. 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
BAA08486.1|AA1_3|1.10.3.-	0.0	1	605	1	605
QLI68968.1|AA1_3	6.76e-280	19	605	19	601
QIW99253.1|AA1_3	1.03e-257	20	605	38	621
QED41496.1|AA1_3	4.65e-242	17	605	29	613
AEO66253.1|AA1_3	1.44e-236	8	597	11	621

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	9.86e-145	10	605	19	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	2.78e-144	10	605	19	580	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	6.34e-112	38	588	4	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.52e-112	38	588	5	529	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.42e-111	24	588	20	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q0CCX6|GEDJ_ASPTN	0.0	1	605	1	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q4WQY8|TPCJ_ASPFU	1.64e-306	1	605	1	609	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.24e-270	28	605	26	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	1.70e-150	14	605	30	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.10e-140	14	605	28	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.504674	0.495338

TMHMM  Annotations     

There is no transmembrane helices in ATEG_08458-t26_1-p1.