CAZyme Information: RAK79067.1

Basic Information

• Species: Aspergillus fijiensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fijiensis
• CAZyme ID: RAK79067.1
• CAZy Family: GH5
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
592	KZ824634|CGC4	66024.49	4.8576

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfijiensisCBS313.89	12336	1448319	318	12018

• Gene Location: location=KZ824634:91083-92984(+)

Full Sequence      

MKAVLYTFLAYVTGWTGMQGFWETSDQAVFQTCDNTPTSRHCWGEYSIDTNYYTTVPTTG
HTVEVWLSVQEGICNQDGYNRPCMTFNGTMPGPLITANWGDELVIHVTNNLKSNGTSIHW
HGVRQHNNVHNDGVPGVTQCPITPGETFTYRFQATQYGTTWYHSHFSLQYAEGLFGPLVI
QGPATANYDEDLGTLFLQDWSHTPSYIDWTAKEKYGMTKSQNNLLINGTNTFDCLSSDSA
DANCVGGGRKFEAVFEPGKKYRLRLINVAVDSQFQFSIDGHTLTVISTDFVPIEPYSTDN
VLINVAQRYDVIVEANAPPGDYWLRAGWVKSCAGVANDHPDDSTGIVRYSTGSRRSQIQS
LPTSVSHVQPPAVCLDEPLDRLVPHLQLDVTNITGTTVEDINVRLTGASFFQWTINSSSF
MLDWNRPTLMQIFDGETTFPSQSNVVKVDKKSPTESNEWAVLVIENKAVALLGAIAHPIH
LHGHDFWILAQEGATWDGTTTSWETVNPPRRDTAILPARGHLVIAFQLDNPGAWLVHCHI
AWHAGQGLALQFVENQRDITLQAAERSGFDETCDKWDYWWATAPYPQDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	50	356	1.6e-129	0.9551282051282052

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.03e-74	77	554	16	523	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	2.23e-71	66	554	36	546	L-ascorbate oxidase
259923	CuRO_1_MaLCC_like	6.07e-68	60	180	1	121	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.
259968	CuRO_3_MaLCC_like	7.89e-67	390	553	3	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.
215324	PLN02604	2.96e-65	77	554	39	546	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATZ57071.1|AA1_3	2.23e-226	27	592	33	581
AAK77953.1|AA1_3	2.23e-226	27	592	33	581
QBZ63059.1|AA1_3	5.55e-226	31	592	40	597
ABM21605.1|AA1_3	4.05e-225	23	592	33	584
CAM12502.1|AA1_3	8.44e-224	32	592	36	581

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	9.23e-224	24	592	30	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	1.86e-223	24	592	30	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	2.64e-143	35	585	29	562	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.23e-142	35	585	1	534	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.27e-142	35	585	2	535	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	3.97e-227	27	592	33	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	5.65e-202	31	592	35	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	4.07e-186	33	592	44	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|P06811|LAC1_NEUCR	1.34e-129	35	592	56	606	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|D4APX3|LAC1_ARTBC	4.47e-128	45	592	82	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.072605	0.927366	CS pos: 20-21. Pr: 0.6544

TMHMM  Annotations     

There is no transmembrane helices in RAK79067.1.