CAZyme Information: EXJ70529.1

Basic Information

• Species: Cladophialophora psammophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora psammophila
• CAZyme ID: EXJ70529.1
• CAZy Family: GH3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
706	AMGX01000009|CGC4	76547.92	5.9377

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CpsammophilaCBS110553	13421	1182543	0	13421

• Gene Location: location=AMGX01000009:1143719-1145991(+)

Full Sequence      

MRTSLFPALLGAVFVESVLAGQPGPLGKWMGGGDDCPWGSRTASGSHPQNDMPDTGVTQY
YDFTVARGTYAPDGVQQAMIVVNGQYPGPLIEANWGDWIEVNVHNQIYGPEEPTSIHWHG
LNQPGTPYYDGVVTVAQCPIVPGGNLTYRFRADEYGTSWWHAHYSAQYSSGVVGPIVVHG
PNDASYDVDLYPILVTDWFHDSYEDIVSLVMSPSASGLPFRPFSDSNLVAGVGQYPCANI
TNGAPCSVVPYASWEFEPGKTYRMRFVNTGASAFETISIDGHQLTVIANDFVPVQPYQTE
FVTIGVGQRVEVLVTANQAPGSYWLRAFNSPCGDTNGPYGQGIIYYTGSDPSTPPTSTGA
QPPINSNCQNDPLATTVPQYVMPAAEPDTTITITIAGAPDASGVFHWTMNGVSYDGDLSN
SLLLEAISGQTEFAPQYNVYNTGTNGTVRIIIINTTPAPHPMHIHGHDFQVLAEGFGTWD
GTVTNPTNPQRRDVHMLWAQATPDNPSYIVVQYTQDNAGVWPVHCHIAWHLSAGMVIMLL
EHPEQLTSIQVPESVTQTCPAYTTWYAANPGVVVDDSLRKRTLGEKMVEYMKGGDKEHVQ
HLDKHRNKRGVRGYRGYGHNATAEEFPAHGKFKGNATAHGHGAAHGTEDASYSTMHSKHS
SSTSSHGGKVSPTPSWSTRPQTGTVGKNLAHESKSTGRPGRKRDEV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	49	368	2.6e-112	0.9839743589743589

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.10e-68	58	549	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.
259923	CuRO_1_MaLCC_like	6.52e-64	56	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.
215324	PLN02604	2.82e-63	71	555	37	558	oxidoreductase
274556	laccase	2.93e-62	58	559	3	539	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.
177843	PLN02191	1.24e-61	61	541	26	546	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIW99529.1|AA1_3	8.66e-186	11	578	87	663
QSZ30962.1|AA1_3	1.14e-176	34	578	51	595
APA07098.1|AA1_3	1.67e-176	37	576	54	591
AHC30245.1|AA1_3	2.21e-176	37	575	55	591
UJO18649.1|AA1_3	8.43e-175	37	578	135	685

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	1.59e-101	52	570	17	533	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.64e-101	52	570	18	534	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	2.47e-101	52	570	45	561	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
6F5K_A	1.51e-96	51	578	26	559	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
3V9E_A	1.90e-96	51	563	60	568	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|A0A067XMP2|PTAK_PESFW	2.78e-139	37	578	44	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	5.57e-112	38	577	54	588	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q12570|LAC1_BOTFU	8.77e-100	38	570	47	553	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|P78722|LAC2_PODAS	1.61e-99	53	592	73	620	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q96WM9|LAC2_BOTFU	6.72e-97	53	541	63	543	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000195	0.999756	CS pos: 20-21. Pr: 0.9814

TMHMM  Annotations     

There is no transmembrane helices in EXJ70529.1.