CAZyme Information: OTA28625.1

Basic Information

• Species: Hortaea werneckii
• Lineage: Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
• CAZyme ID: OTA28625.1
• CAZy Family: GH16
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
550	MUNK01000157|CGC1	59800.60	4.2134

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

• Gene Location: location=MUNK01000157:82386-84234(-)

Full Sequence      

MRKFFAGASIVAFCHSACAAVLRSADQSSKFVGTAIPIELGGSDPSLSSRSACSGNTASN
RTTWCDYNISTNYYDVVPDTGATVLTVNGSIPGPTIQANWGDTVKVHVTNSLANNGTSLH
FHGIRQNYTNAMDGVASITQSPVAPGESITYTWRATQYGSSWYHSHYDLQAWEGVLGGIV
INGPSTANWDTDLGMLFLNDWSHQTVDELYTYAETEGPPTMDNGLINGTNTGDDGGSRFN
TSVTEGDIYLLRLINGAADTHFDFMIDNHTLQVISSDFVPIQPYYTDVLSIGMGQRYDVL
VTANMSSVASDFWIRAIPDSYCSESDNTNDIKGILHYGSSTGTPNTTAFTYDSNDCSGED
APDIVPYLALDAENTDNLYKWYIGGTTFLVDWSNPTGRKLTTNETTSFADSNAVIELATA
DEWYYLIIETTLAVPHPIHLHGHDFWQLASGTGTYASSNATLNTSNPPRRDTAMLPGSGY
LVIAFKADNPGAWLCHCHIAWHTSEGFALQSVERRDEIPALYDTAQMNSTCSAWDAYLNS
TDLEQDFSGV

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	63	356	1e-114	0.9583333333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259968	CuRO_3_MaLCC_like	5.17e-74	362	512	4	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.
225043	SufI	2.98e-62	74	506	44	441	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].
274555	ascorbase	2.28e-61	84	519	22	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.
259947	CuRO_2_MaLCC_like	1.76e-60	193	351	1	164	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.
274556	laccase	2.88e-59	84	509	24	515	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO13577.1|AA1_3	1.30e-250	46	550	39	579
AFG30950.1|AA1_3	1.60e-249	4	550	5	571
AFG30951.1|AA1_3	1.60e-249	4	550	5	571
UKZ68800.1|AA1_3	2.91e-234	45	550	28	566
UKZ52917.1|AA1_3	7.79e-232	21	550	12	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5LWX_A	1.10e-177	55	537	22	556	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	9.86e-177	62	537	2	528	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.02e-176	62	537	3	529	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3SQR_A	1.48e-154	34	550	20	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	1.48e-154	34	550	20	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96WM9|LAC2_BOTFU	8.65e-156	34	550	20	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	3.43e-150	47	550	31	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	3.66e-137	64	550	54	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96UM2|LAC3_BOTFU	7.77e-121	92	510	1	451	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|Q03966|LAC1_CRYPA	2.38e-113	56	550	37	591	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.016757	0.983235	CS pos: 17-18. Pr: 0.8961

TMHMM  Annotations     

There is no transmembrane helices in OTA28625.1.