CAZyme Information: EXJ76688.1

Basic Information

• Species: Cladophialophora psammophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora psammophila
• CAZyme ID: EXJ76688.1
• CAZy Family: GT76
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
716	AMGX01000001|CGC7	78290.15	6.0059

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=AMGX01000001:3386988-3389817(+)

Full Sequence      

MDTQPPLALREETRRPPQPILLQEARARLLALLEAQLQAILQWDRDRHRARLDLLAAQLQ
AILQWDRERHRARLALPEAQLQLILLLELRPRLLLLEAQLQAIPRLAPAQHPALPLIPQL
EPQPRPLPAPLTLLWCGKSVGDDTDEPYTTGETKSYTFTITDANINFDGTVRPSFAINGG
TPGPLIEVNWGDTVEITVINLLTDNATTIHWHGIRQIGTNDQDGVPGVTECAIPPGGSRT
YTWLASTYGTGWYHSHALSQYGGGIRGPVIIHGPATANYDYDMGHVMIDEIFSQTIFQMA
WNIARLRGPLPAAVNYMVNGKNKSPDGSTGQATQWTVEAGKKHLFRIINSSAQSSFIVHF
DYHEMTVISSDYTPIVPYKTTSLYVNPGQRYNVIVEMNQTPGAYFMRAITQTGCGAQNVN
NGLGIANPVFTYKGTCGTPTSETLSLTPASDCKDEPLASLVPYVSKDGGSAEDFTDTAKL
LPGGNGGSQTFAGYGPIIRWYFGGLLDLAGNSATALGNQTITVDFENPTLRTMAELPTLS
FNSSRYSNAVVLDGPPGDWVYFVIQNNFQTSHPIHLHGHDFSVLGQGKGVFTAAQVSSLN
FANPCRRDTALLFGFAGPGGVAQGGWTVIGFQTDNPGAWVMHCHIIWHADGGMGLQYIEQ
PDAIDANGYWSSQGFQDECNAYTTYADGGGEGRLSYEAGIKRDLERHKYALHHGMH

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	148	445	4.7e-106	0.9551282051282052

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	6.94e-68	151	272	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	3.49e-57	168	661	48	450	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].
274556	laccase	1.87e-56	151	658	1	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.
274555	ascorbase	6.11e-54	168	659	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.
259968	CuRO_3_MaLCC_like	1.33e-53	516	658	28	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAK03309.1|AA1_3	6.23e-287	135	714	232	810
QIX00022.1|AA1_3|CBM20	4.45e-123	137	682	98	612
SMY24903.1|AA1_3|CBM20	1.09e-118	139	688	185	714
SMQ51259.1|AA1_3|CBM20	1.09e-118	139	688	185	714
SMR54833.1|AA1_3|CBM20	1.09e-118	139	688	185	714

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LM8_A	5.92e-105	150	686	20	529	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.10e-105	150	686	21	530	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3V9E_A	7.20e-105	150	683	64	568	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	1.31e-104	150	686	48	557	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
3SQR_A	1.99e-104	150	683	64	568	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J5JH35|OPS5_BEAB2	3.12e-114	150	661	70	553	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	9.02e-110	182	657	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q12570|LAC1_BOTFU	2.42e-107	148	685	57	548	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q96WM9|LAC2_BOTFU	2.92e-103	150	683	65	569	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|P06811|LAC1_NEUCR	1.84e-100	150	685	81	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000030	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EXJ76688.1.