CAZyme Information: PMAA_072680-t26_1-p1

Basic Information

• Species: Talaromyces marneffei
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei
• CAZyme ID: PMAA_072680-t26_1-p1
• CAZy Family: GH5
• CAZyme Description: multicopper oxidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
585	DS995900|CGC16	64787.69	4.7513

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmarneffeiATCC18224	10194	441960	145	10049

• Gene Location: location=DS995900:3010716-3012655(+)

Full Sequence      

MQLVILISLLSVAGLCSCDSESISGLSPWGTLPSPNLPSWIDFIGVNQWNTNAHQNVVPS
TGKIRKYNFDIRREYAAPDGVNKSVILINDQYPGPLIEADWGDIITVTVTNNIDVGTEEG
VTLHWHGLTQKNTPWMDGVPGVTQCPIVPGGSFTYTFQADQFGSSWYHSHYSAQYNDGLF
GPIVIHGPVQSGYNYDFDLGPIMISEYTHTSYYESLEMLFEYPPAFPNVDNNLINGKGAF
DCQSNCDEGPSLAKFKFTSGKKHRLRLINTGMTANQKFSIDGHELTVIANDFVPVQPYKT
NVVTLGVGQRTDVIVEATGNPSGVYWMRSDIDMDCLNMTSTIPNATAIIYYEHANLSAIP
TTTATPWTSNECRNDPLESTVPYYPQTPPTYPAITQELLIELKPNASGAFLMYVNNVSTR
VNYDNSVLLDAKAGIPSSSLDPELSIYDFGSNSSVRMVIYNTWGQQHPMHLHGHNFWVLA
EGKGTWDGTVTNPNNPQRRDTHLMMPGSTDTPSYIVLEWELNNPGVWPMHCHMSTHASGG
LIINTLEQPSSIQKQLKIPRAIPETCINWAFFAGHDYIDQIDSGV

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	55	372	5.3e-124	0.9839743589743589

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.96e-76	64	562	1	535	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.
215324	PLN02604	1.99e-70	60	562	20	558	oxidoreductase
259923	CuRO_1_MaLCC_like	4.93e-70	62	186	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.
177843	PLN02191	9.96e-70	60	554	19	553	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	2.15e-61	387	546	1	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
QGA18227.1|AA1_3	0.0	1	585	1	585
BCS07898.1|AA1_3	2.25e-261	11	585	14	602
BCR95349.1|AA1_3	1.52e-260	25	585	52	626
QKX63435.1|AA1_3	1.22e-239	24	584	17	583
CAK48652.1|AA1_3	2.88e-234	49	585	106	648

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	3.48e-107	58	585	61	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	6.90e-107	58	585	61	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	2.29e-95	34	577	27	566	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	5.93e-95	50	577	10	538	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	6.10e-95	50	577	11	539	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|A0A067XMP2|PTAK_PESFW	1.49e-172	52	585	52	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	5.29e-112	50	585	60	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.15e-108	56	585	60	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	6.99e-104	50	585	53	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|A0A067XMP0|PTAE_PESFW	4.73e-96	62	585	55	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001319	0.998685	CS pos: 18-19. Pr: 0.5893

TMHMM  Annotations     

There is no transmembrane helices in PMAA_072680-t26_1-p1.