CAZyme Information: TRIREDRAFT_122948-t26_1-p1

Basic Information

• Species: Trichoderma reesei
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei
• CAZyme ID: TRIREDRAFT_122948-t26_1-p1
• CAZy Family: CE16
• CAZyme Description: predicted protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
568	GL985071|CGC3	63357.14	6.4996

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TreeseiQM6a	9138	431241	7	9131

• Gene Location: location=GL985071:658024-659931(-)

Full Sequence      

MSLWPVADFLRNKPTAPFLPDFLNNNPTPNGFPWSHYGIHTNYYNTSPNTGVLRSYDFTI
SRGVIAPDGYQRNVLLINGAFPGPLIEANWGDTIQVTLHNNITGPEEGTALHWHGFLQQG
TPWEDGAPAVTQCPVAPGKSFTYQFVASLYGSTWYHSHYSSQYAGGLVGPLVVHGPKSRN
YDVDVGPVMLSDWYHDTYFDLVEKTMSTVPGEAFFPSDNNLINGKMFFDCSQVTDGTPCT
NNAGISKFRFRRGKTHLLRLINAGAAGLQRFSIDGHKMTVIANDFVDVEPYETKVVTLGI
GQRSDVLVKADGDLDAYWMRSNISSCAFTRQPNALAAIYYDNADTNAEPRSTPWDVPDSG
ICVNDDLSLTEPVMKLPLPKPDLTIDMEMDQYQNETGHRLWRMDGVSFRGNFNSPTLLLS
NLGNHTFDPQWSVKNTGDAKSVRVNLINHSGAPHPMHLHGFNMYILHEGPGEWDGKTIIR
PSNPQRRDTFMVRAGGHVVMQFDAASNPGVWPFHCHIAWHASAGLFTQFLTAPREVRKLR
IPNVVAETCRQWGRWTNTNIPEQIDSGL

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	41	358	8.2e-123	0.9871794871794872

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
215324	PLN02604	6.10e-71	53	539	24	554	oxidoreductase
274555	ascorbase	2.17e-70	54	539	2	531	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.
259923	CuRO_1_MaLCC_like	1.76e-69	51	174	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	1.17e-64	77	533	57	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].
259968	CuRO_3_MaLCC_like	1.53e-62	376	530	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
ACS45199.1|AA1_3	0.0	15	568	36	590
UKZ94937.1|AA1_3	0.0	15	568	36	590
UKZ56777.1|AA1_3	0.0	15	568	35	588
UKZ72019.1|AA1_3	0.0	16	568	37	590
QYT04556.1|AA1_3	0.0	19	568	2	551

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	3.12e-110	34	568	49	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	6.20e-110	34	568	49	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	1.81e-104	24	559	23	560	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	3.26e-104	33	559	3	532	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	3.35e-104	33	559	4	533	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	4.18e-186	27	568	38	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|J5JH35|OPS5_BEAB2	1.97e-120	34	568	54	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	1.42e-114	34	568	49	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q0CCX6|GEDJ_ASPTN	1.83e-104	51	568	57	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q4WQY8|TPCJ_ASPFU	2.88e-104	19	568	24	609	Oxidoreductase tpcJ OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=tpcJ PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000055	0.000001

TMHMM  Annotations     

There is no transmembrane helices in TRIREDRAFT_122948-t26_1-p1.