CAZyme Information: AN5397-T-p1

Basic Information

• Species: Aspergillus nidulans
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans
• CAZyme ID: AN5397-T-p1
• CAZy Family: GH36
• CAZyme Description: Putative multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
664		74426.13	4.7423

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=ChrV_A_nidulans_FGSC_A4:2943944-2945993(-)

Full Sequence      

MLRSSFLLFFYALYASASWVFEHDFQPEERSLLFGTDVSPLKRRQEEGSSSASDSILSVA
GGGGGRSSGRPQPTSTSFTQTRTTSTRPTSTNTRTGTRSSSNTTTRTSTSATSTPTTTAT
GTPCAGNTPDTRREWCDYSIDTNYHDITPDTGVVREYWLELDEITVSPDGISRPAVAVNG
TIPGPTIFADWGDEVVVHIKNNLHETLNGSTIHWHGIRQLNTNEHDGVVSITQCPITPDH
EYTYRWRAQQYGTTWYHSHISLQAWDGVVGPIIINGPATENYDVDAGTIFLNDWTHQTFE
ELFWYAQIVGPPLLNNSLINGTGVYGSSFSGHRAKGQKETGERFSMKVEEGTSYRLRLIN
GAIDTHYKFMIDSHELTVIAMDLVPVKPYKTTAVSLAMGQRYDVIVTANQRSKSDSFWLR
SIPQQSCSDVEDPGNIRGIFYYGDRPSTPKTEPYPFEDSCMDEPMASLVPHVARDVQPPD
YQNNALASVSFNEDHFFRWFLNSTTMQVYWEDPTLLQILNGDDSFENSSAVIELPNANEW
VYMIVNTTIPVSHPIHLHGHDFFILAQGTNPWDGKYQTSNPPRRDTAVLPGNGYLVMAWE
TDNPGAWLMHCHIGWHTTEGFALQFVERIDEIRENVDRDFVVNACNTWNGYGEEYGVEQY
DSGV

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	142	460	1.9e-129	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	3.92e-73	478	626	6	157	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.
274555	ascorbase	5.69e-65	154	634	1	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.
274556	laccase	1.66e-64	154	626	3	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.
259923	CuRO_1_MaLCC_like	9.10e-64	152	275	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.
225043	SufI	3.32e-62	169	626	48	447	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].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAA62557.1|AA1_3	0.0	1	664	1	664
AWI47683.1|AA1_3	0.0	15	645	1	633
BCS27040.1|AA1_3	9.91e-318	121	664	37	577
QQK45664.1|AA1_3	2.83e-265	121	664	54	591
CAP98129.1|AA1_3	1.44e-264	121	664	70	607

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.27e-172	122	664	36	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]
3V9E_A	1.27e-172	122	664	36	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	1.21e-166	127	664	29	577	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	5.47e-166	127	664	1	549	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	5.65e-166	127	664	2	550	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|Q96WM9|LAC2_BOTFU	1.19e-172	122	664	36	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	2.99e-167	129	664	48	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	2.29e-150	124	664	37	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|P06811|LAC1_NEUCR	2.70e-120	127	651	56	592	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
sp|Q70KY3|LAC1_MELAO	5.61e-117	127	664	55	609	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.503579	0.496415

TMHMM  Annotations     

There is no transmembrane helices in AN5397-T-p1.