dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: SPSK_04101-t39_1-p1

You are here: Home > Sequence: SPSK_04101-t39_1-p1

Basic Information help

Species

Sporothrix schenckii

Lineage

Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii

CAZyme ID

SPSK_04101-t39_1-p1

CAZy Family

GH16

CAZyme Description

laccase TilA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
641		69644.81	5.9495

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sschenckii1099-18	10434	1397361	141	10293

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	1.10.3.2:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA1	69	269	1e-50	0.5167597765363129
AA1	323	620	2.3e-28	0.4972067039106145

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.04e-75	467	626	2	164	The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), 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 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.
259919	CuRO_1_Abr2_like	2.82e-60	55	170	1	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. 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. Laccase 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. Like other related multicopper oxidases (MCOs), 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
215324	PLN02604	9.45e-56	50	634	22	555	oxidoreductase
274555	ascorbase	2.20e-55	52	634	1	532	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.
177843	PLN02191	2.45e-49	60	634	27	555	L-ascorbate oxidase

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
3.72e-218	53	640	41	632
1.12e-195	47	640	24	638
3.45e-191	51	639	27	601
6.60e-191	55	637	34	600
2.78e-190	56	639	32	601

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
6.98e-44	54	627	5	468	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
3.54e-43	34	625	13	488	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
1.62e-42	54	629	5	470	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
2.33e-42	54	627	5	471	Chain A, Laccase [Trametes versicolor],1KYA_B Chain B, Laccase [Trametes versicolor],1KYA_C Chain C, Laccase [Trametes versicolor],1KYA_D Chain D, Laccase [Trametes versicolor]
3.00e-42	50	621	65	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.13e-127	55	641	22	584	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
1.35e-125	57	638	27	611	Laccase 1 OS=Metarhizium anisopliae (strain ARSEF 549) OX=1276135 GN=Mlac1 PE=2 SV=1
1.44e-125	57	638	28	612	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1
2.77e-125	57	638	27	611	Laccase 1 OS=Metarhizium guizhouense (strain ARSEF 977) OX=1276136 GN=Mlac1 PE=3 SV=1
3.91e-125	57	638	27	611	Laccase 1 OS=Metarhizium acridum (strain CQMa 102) OX=655827 GN=Mlac1 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.013900	0.986077	CS pos: 20-21. Pr: 0.9271

TMHMM Annotations help

There is no transmembrane helices in SPSK_04101-t39_1-p1.