CAZyme Information: OAG15405.1

Basic Information

• Species: Alternaria alternata
• Lineage: Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
• CAZyme ID: OAG15405.1
• CAZy Family: AA8
• CAZyme Description: laccase-1 precursor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
561		61299.33	3.9054

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f	13577	N/A	111	13466

• Gene Location: location=KV441494:475639-477502(-)

Full Sequence      

MLLRCIFSIAALAGYATAFPFTSDLRPRAACDGNTATTRSEWCDYSIDVDPSDDVPDTGV
TREYWLELTDVTVAPDGVSRSAMAVNGSIPGPTLIADWGDTVVVHVTNSLTTSNNGTSIH
FHGIWQLNTNDQDGVSSITQCPTAPGESMTYTWRATQYGSSWYHSHFALQAWQGVFGGII
INGPATANYDEDLGVLMLNDWDHQTVDELYITAETSGPPTLDNGLINGTNTYEDGGYRFN
QSFTSGTSYLFRLVNAAVDTHWKFMIDNHTMTVIASDLVAIEPYEATVISIGMGQRYDIV
VTADQTDATDFWMRAIPQSACSENDNEDDIRGIIYYGDAPGTPTTSAYDYEDSCSDETDN
IVPYVSKTVGSTAGATADEPVAVGFNSDNLFKWTLNSTTFVSEWEDPTLMKIMQGETAFE
TSNAVFLLPNANEWVYVVISTTLAVPHPIHLHGHDFYVIAQGTGTYTDGETTLNLDNPPR
RDTAMLPASGYLVLAFETNNPGAWLMHCHIGWHTSEGFAMQFVEQYDAIAGITSNDTLIS
NCDSWTSHTETVGIEQDDSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	52	354	4.6e-129	0.9839743589743589

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	1.03e-76	381	523	14	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	6.46e-66	61	532	1	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	8.42e-66	58	532	20	554	L-ascorbate oxidase
274556	laccase	3.16e-65	61	523	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	6.44e-65	59	182	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFG30950.1|AA1_3	4.00e-317	20	561	30	571
AFG30951.1|AA1_3	4.00e-317	20	561	30	571
CAE7032522.1|AA1_3	7.91e-311	1	561	1	567
QOU09627.1|AA1_3	2.37e-299	2	561	1	571
UQC89044.1|AA1_3	6.47e-293	23	561	31	574

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	3.30e-175	23	561	27	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.30e-175	23	561	27	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]
5LWX_A	9.66e-174	27	548	17	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.51e-172	42	548	4	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.63e-172	42	548	5	529	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	3.82e-176	16	561	19	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	2.70e-163	17	561	23	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	2.82e-148	38	561	50	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	9.13e-134	90	522	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q03966|LAC1_CRYPA	1.34e-125	25	561	28	591	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000340	0.999642	CS pos: 28-29. Pr: 0.8586

TMHMM  Annotations     

There is no transmembrane helices in OAG15405.1.