CAZyme Information: PMAA_100410-t26_1-p1

Basic Information

• Species: Talaromyces marneffei
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei
• CAZyme ID: PMAA_100410-t26_1-p1
• CAZy Family: GT32
• CAZyme Description: multicopper oxidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
392	DS995902|CGC30	44579.89	5.1959

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=DS995902:2769620-2770852(+)

Full Sequence      

MQYGTGWYHSHYSLQYINGAYGPVVIHGPTSTNYDHELEPLLISDWYHADAFSMFHEEIT
DHAHIPTGTLMNGKGVFDCDPDEDTRCTGKEVRHEIVFEPGKKHKLRLVNSGSLATYKFW
MDGHNFTVVANDFVPIEPYVTDVLILGIGIFSFYCWFTDSIANMWLTQRYDVIIEANATL
EYGSNFWMHATHCDDEMPVPWDTRIGIIRYNTNDKSNPYTPSASTHHPGYGCRDPDPSSL
RPIVKRQVGKEVNGMCPSEYLKIGLQSWPNISDPDSVIRKWVLANRSQSVDWHDPSLMQV
VSHDKVNLTEEAAPINLDYETGEWVYFVIEGNFTDINDPPRPIPRSVHPIHLHGHDFVIL
AQGDGEFTSDIVPNLNNPARRDRVNCPIGGYV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	149	1.5e-54	0.46153846153846156

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259947	CuRO_2_MaLCC_like	1.28e-64	38	224	1	167	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.
259968	CuRO_3_MaLCC_like	1.91e-33	257	392	8	126	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.
259868	CuRO_2_LCC_like	1.70e-32	40	210	2	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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.
259953	CuRO_2_MCO_like_1	2.33e-28	41	211	3	163	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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.
395317	Cu-oxidase	3.01e-23	40	190	4	125	Multicopper oxidase. Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA18836.1|AA1_3	8.14e-272	16	392	101	457
QED41496.1|AA1_3	7.70e-216	1	392	159	536
QLI68968.1|AA1_3	1.20e-159	1	392	151	524
QIW99253.1|AA1_3	1.28e-142	2	392	169	544
BAA08486.1|AA1_3|1.10.3.-	7.98e-129	2	391	154	527

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.11e-64	2	392	161	510	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	1.11e-64	2	392	161	510	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	1.81e-48	2	382	117	455	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.84e-48	2	382	118	456	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	3.84e-48	2	382	145	483	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q0CCX6|GEDJ_ASPTN	7.10e-130	2	391	154	527	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.18e-126	2	392	153	533	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|Q4WQY8|TPCJ_ASPFU	1.64e-123	2	392	155	532	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	2.15e-73	2	392	167	519	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|D4APX3|LAC1_ARTBC	1.08e-64	2	392	185	553	Laccase ARB_05828 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_05828 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000024	0.000012

TMHMM  Annotations     

There is no transmembrane helices in PMAA_100410-t26_1-p1.