CAZyme Information: TSTA_082980-t26_1-p1

Basic Information

• Species: Talaromyces stipitatus
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
• CAZyme ID: TSTA_082980-t26_1-p1
• CAZy Family: GH39
• CAZyme Description: multicopper oxidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
554	EQ962653|CGC11	62976.15	6.5344

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TstipitatusATCC10500	12629	441959	146	12483

• Gene Location: location=EQ962653:692810-694876(-)

Full Sequence      

MYLDYDRVESSIFFLFAFLANLLPWSTPKPVPFAIQEPISTQSPSTREIRKYNFTIKRGI
FPGPLIEANYGDTISVTVHNEIEDPEEGTALHWHGILQKGTPWFDGVPGVTQCPIAPGKS
LEYTFKAEPYGTSWYHAHYSAQYANGIFGAMVIHDPKHVNYDIDMGPVLLTDYFHRYYRD
VVLEVLRPRPFPAAPPSDLNLINAKGDWRCTDSLGSAPSPDTHNLTEFRLEPGKKHLLRL
INAGAEGMQRFSVDNFTLEVIANDFTPLQPYNTNVVTLAVGQRVDGVLTVPEDHVEPVWV
RSYISDLCSFTNHHSAHAVAYFTDDIIDVMPSTSGHPIDDSDCGGYYQTFLSHCRRKRAQ
SFQGARDWKYYERHRTMGLAYEWLRRRSGPNESSVVSCQQRRAKLRHQWNVFDTGKARTI
RVFLKNPIDFPHPMHIHGHNVKILAEGVGEWDGTIVNPSNPNRRDTQMIRSLGYMVFEID
DVDNAGLWPFHCHIGPHLSAGFSVTLMRDPDQLAKMTVPYSIKQTCVDWIALKDRVPDQI
DSGLQVDAFETEKI

Enzyme Prediction     

EC	1.10.3.2:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	54	502	1.7e-94	0.9664804469273743

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	3.83e-58	50	154	4	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.
259947	CuRO_2_MaLCC_like	1.48e-57	165	340	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.
177843	PLN02191	2.94e-49	59	516	49	554	L-ascorbate oxidase
259926	CuRO_1_Diphenol_Ox	3.87e-48	50	154	1	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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.
274555	ascorbase	2.26e-46	59	504	27	519	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUC17622.1|AA1_3	8.36e-149	19	544	50	592
QLI66315.1|AA1_3	1.36e-144	44	544	70	592
QYT04556.1|AA1_3	8.46e-144	43	544	30	551
QPC63439.1|AA1_3	4.94e-143	21	544	47	585
QPC72323.1|AA1_3	9.86e-143	21	544	47	585

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.65e-71	21	544	60	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.65e-71	21	544	60	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]
5LWX_A	3.41e-67	44	529	46	553	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.62e-67	44	529	18	525	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.70e-67	44	529	19	526	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	2.47e-122	46	544	61	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	1.61e-76	56	544	97	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.13e-71	56	513	80	570	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2
sp|Q96UM2|LAC3_BOTFU	4.54e-70	62	504	1	450	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q96WM9|LAC2_BOTFU	1.81e-68	46	531	86	567	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.672507	0.327495

TMHMM  Annotations     

There is no transmembrane helices in TSTA_082980-t26_1-p1.