CAZyme Information: HCEG_05796-t36_1-p1

Basic Information

• Species: Histoplasma capsulatum
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum
• CAZyme ID: HCEG_05796-t36_1-p1
• CAZy Family: GH55|GH55
• CAZyme Description: laccase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
597		66620.72	6.2400

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumH88	9666	544711	221	9445

• Gene Location: location=DS990639:4489516-4491836(-)

Full Sequence      

MTLRKNAASSLSVIIYIFWVLLGSSICAAQSNTYHPIPEKGPLGYVSDKNCKHGPTNRAC
WGGGFDVATNFGVKWPDTGKVVEYHLEITNTTLAPDGFERLVLAVNGQFPGPTIRAEWGD
TVRIHVKNNMQNNGTSIHWHGIRQKYTNQQDGTNGVTECPIPPGGSKTYEFKCTQYGTSW
YHSHHTVQFVDLKSRRYGDGVLGAIVISGPASANYDIDLGEMSIQDWYYRTAWQNALLGI
PPVADNGLINGTMVNANGGGKYHENVIKKGKSYLLRLINTSVDNYFKVHLDNHLFTVVSS
DFVPIMPYQADWLFIAIAGQRYDVIIHADQEIDNYWFRAEVQKGCGQNAMNGKIKSIFRY
EGADPNANPTSVASNYTQGCDDEEGLIPFVPIDVPSDHFSQQAKDLNVSFQSEVSLPGQN
IVHWRINGVPIETDWEYPTLQYVLDCNTSFPQRLNVIPLPEPNVWTYWIIEASFESTVNV
PHPIHLHGHDFSILGTGRGNFPGPEGLNFKNPARRDSVMLPDHGWVAIAFPTDNPGAWLA
HCHIAWHAHEGLAVQFLERSSEIPSALNIAQSWHHTCAQWKDYILDNAIYQQEGSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	69	380	9.8e-124	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	5.92e-74	81	566	1	534	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	3.80e-69	79	207	1	121	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.
177843	PLN02191	9.48e-68	78	564	20	555	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	1.10e-64	410	557	12	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.
215324	PLN02604	1.62e-63	79	567	22	558	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS57203.1|AA1_3	0.0	1	597	1	588
QSS72037.1|AA1_3	0.0	1	597	1	588
QSS61236.1|AA1_3	0.0	1	597	1	589
ALR81978.1|AA1_3	4.43e-212	46	597	115	671
APA14269.1|AA1_3	2.84e-208	46	597	95	652

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GW0_A	5.22e-154	55	597	7	559	Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],1GW0_B Crystal Structure of Laccase from Melanocarpus albomyces in Four Copper Form [Melanocarpus albomyces],2IH8_A A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH8_B A low-dose crystal structure of a recombinant Melanocarpus albomyces laccase [Melanocarpus albomyces],2IH9_A A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],2IH9_B A high-dose crystal structure of a recombinant Melanocarbus albomyces laccase [Melanocarpus albomyces],3FU7_B Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_A Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU9_B Melanocarpus albomyces laccase crystal soaked (20 min) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3QPK_A Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces],3QPK_B Probing oxygen channels in Melanocarpus albomyces laccase [Melanocarpus albomyces]
3DKH_A	7.38e-154	55	583	7	546	L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]
2Q9O_A	7.38e-154	55	597	7	559	Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],2Q9O_B Near-atomic resolution structure of a Melanocarpus albomyces laccase [Melanocarpus albomyces],3FU7_A Melanocarpus albomyces laccase crystal soaked (4 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_A Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces],3FU8_B Melanocarpus albomyces laccase crystal soaked (10 sec) with 2,6-dimethoxyphenol [Melanocarpus albomyces]
3SQR_A	8.34e-150	50	597	38	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	1.67e-149	50	597	38	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|Q96UM2|LAC3_BOTFU	2.33e-175	110	556	1	452	Laccase-3 (Fragment) OS=Botryotinia fuckeliana OX=40559 GN=lcc3 PE=3 SV=1
sp|P06811|LAC1_NEUCR	3.94e-157	55	597	58	606	Laccase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=lacc PE=1 SV=3
sp|J5JH35|OPS5_BEAB2	1.81e-153	12	597	6	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|P78722|LAC2_PODAS	2.41e-153	53	583	50	592	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q70KY3|LAC1_MELAO	2.05e-152	55	597	57	609	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000307	0.999670	CS pos: 29-30. Pr: 0.9368

TMHMM  Annotations     

Start	End
7	29