CAZyme Information: AN6830-T-p1

Basic Information

• Species: Aspergillus nidulans
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans
• CAZyme ID: AN6830-T-p1
• CAZy Family: GH55
• CAZyme Description: Putative multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
455	ChrI_A_nidulans_FGSC_A4|CGC9	51370.07	6.0468

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnidulansFGSCA4	10988	227321	276	10712

• Gene Location: location=ChrI_A_nidulans_FGSC_A4:3314684-3316243(-)

Full Sequence      

MVLLRHLHSYTTTVPETGVIREYHFNLERITAFSDGRERFALVINDSIPGPTIKAVGVIP
WSSMSQIVCRTASKMAPVCIFTEWRAMQYGTTWYHSHIGLQAWEGLFGGIVIHGPASENY
DKDLGVMFLNYWDISTVDELRDYAQSEGPPTLDNVLINGTNVYGSDEGNKTGRRWNTTFV
KSTSYRLRLVNEAVDTHSKFMVDNYTLTVIANDLVPTQPYETTVLDIAMGQRYDVIITAD
QASVADSFWLRAIPQEACSENESSDNIRDVGLRLHGLLLRRRPLKPHTDGEPAKRLKQRL
LYKSESVTLGTNTENLFRWKLNSTSMHVDWTDPILLEIYRNHSVSTFANTSGVVELPKAN
EWVYVVIETELTVPYPIHLHGHVSVIIAQGTGTYNSSSDNLIDTLGAANLPRRDTAMLKE
TVYLIVGFYTDNPGAWLMHCHIGWHTEEGLRDAVY

Enzyme Prediction     

No EC number prediction in AN6830-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	83	267	2e-68	0.5897435897435898

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	1.08e-60	307	450	14	152	The third 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 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.
259947	CuRO_2_MaLCC_like	5.90e-47	124	268	1	144	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.
225043	SufI	3.83e-30	90	450	126	442	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].
177843	PLN02191	1.17e-27	17	450	20	540	L-ascorbate oxidase
274555	ascorbase	3.61e-26	20	450	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAE54583.1|AA1_3	4.95e-178	9	450	66	543
QRD89294.1|AA1_3	6.78e-178	9	450	66	542
QMW24812.1|AA1_3	6.78e-178	9	450	66	542
QMW36814.1|AA1_3	5.49e-177	9	450	66	542
UCK57132.1|AA1_3	5.49e-177	9	450	66	542

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	2.84e-115	9	454	40	530	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.41e-114	9	454	12	502	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.46e-114	9	454	13	503	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3SQR_A	1.42e-96	14	450	61	536	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	2.81e-96	14	450	61	536	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|Q96WM9|LAC2_BOTFU	2.94e-95	9	450	57	537	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	1.14e-85	9	450	62	545	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	3.58e-83	9	450	56	515	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96UM2|LAC3_BOTFU	8.03e-77	85	450	63	448	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|P06811|LAC1_NEUCR	3.12e-68	9	452	73	561	Laccase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=lacc PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000000

TMHMM  Annotations     

There is no transmembrane helices in AN6830-T-p1.