CAZyme Information: PV07_05216-t44_1-p1

Basic Information

• Species: Cladophialophora immunda
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora immunda
• CAZyme ID: PV07_05216-t44_1-p1
• CAZy Family: GH15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
644		72439.64	6.8577

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CimmundaCBS83496	12879	N/A	49	12830

• Gene Location: location=KN847042.1:2122186-2124327(-)

Full Sequence      

MVSIWARIVAVFHFILLSPPKEEGPDQRPLSASVHAAFPPQVTVQADDHQAPTPFLPPSA
PRASNFTCEYPDLDGYTFCSTYGDRSCWLKHPDPQKQVYDINTDYENVFPKGKTRQYYIE
VNEKTIRPDGVDRKAMVVNDTYPGPWIEACWGDWLEITVKNNLKTNGTTIHWHGIRQLHT
TASDGVNGITQCPIAPGETYTYRFRAMQYGTTWYHSHYSLQYGEGVLGPMTIHGPASADY
DEAQPPVLMTDWTHESWYTKWWDNVINGKARPEPDNILVGGKGTWPASKPSKGFRLDFVK
GTRYLLRLINTSVDTSFVFSIDNHKIQVIGSDLVPIVPYITDHVVVGIGQRYHIIVTANP
RDGKANATYWIRTQPAKGCDPGGTSKIDPRTGIVVYKDTEPVDYPVTFDTTCRDEPYDKL
VPILKWTVGRPSNIAANSQFDIGFDQITAGTEYPANLTRGRFNMYSDTMWLNFTNVTLSQ
NLSAPQAAFNSHSVAVKENSQKDDWVYLLVSGTGIPRSGRTYLPIAHPIHLHGHDFAILQ
QSTKPYRIGGLDLKLDNPPRRDVAFMPRDGYLVLAFKADNPGVWLMHCHIATHASGGLAM
QIVENGNQTVLDPFDQKQLAHTCKKWKDWASDKDHRFLQDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	103	411	6.7e-125	0.9903846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	1.02e-73	112	233	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.
274556	laccase	2.55e-63	112	613	1	532	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.
274555	ascorbase	2.49e-59	114	593	1	512	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	3.88e-59	115	608	24	550	L-ascorbate oxidase
259947	CuRO_2_MaLCC_like	5.00e-57	245	412	2	165	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD61993.1|AA1_3	2.25e-195	9	644	15	658
QGI68425.1|AA1_3	9.05e-195	9	644	15	658
QGI99317.1|AA1_3	9.05e-195	9	644	15	658
CCT72796.1|AA1_3	1.28e-194	9	644	15	658
QGI85635.1|AA1_3	1.28e-194	9	644	15	658

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.22e-141	85	644	46	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	2.43e-141	85	644	46	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	8.55e-122	92	630	28	557	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LWW_A	4.23e-121	92	630	1	530	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LM8_A	1.15e-120	97	630	5	529	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4APX3|LAC1_ARTBC	6.97e-166	39	644	23	633	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	1.45e-139	85	644	46	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	2.49e-127	85	644	51	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	3.57e-121	85	644	35	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q12570|LAC1_BOTFU	2.14e-120	85	644	44	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001499	0.998477	CS pos: 23-24. Pr: 0.6873

TMHMM  Annotations     

There is no transmembrane helices in PV07_05216-t44_1-p1.