CAZyme Information: jhhlp_003954-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_003954-t41_1-p1
• CAZy Family: GH10
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
593	NLAX01000010|CGC10	65209.75	5.2535

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LprolificansJHH5317	8768	N/A	208	8560

• Gene Location: location=NLAX01000010:2397177-2399408(+)

Full Sequence      

MRSFALFQAVGLFLGLGNAAPSPIDVAVAPRELVKRAPTCNTPSNRACWSDGFNINTDYE
ASIPDTGVTRHYDFTVSQFENWIGGDGIEKKVAMLINGQFPGPTVRADWGDWVEIKVTNN
LTCDGTSIHWHGIRMRGNSVNDGANGVTECPIAPGTSKTYRFRAEQYGTGWYHSHYSAQY
ANGLLGTVVIDGPASLPYDEDLGVFPINDWYYGDAEEIGRGLIPPPGAAPAADNVLFNGT
HVNAQGGGEYARVVLKAGKRHRLRLINPSVDISYSVTLANHDLTVISTDFVPVNAFTTPS
VFLNPGQRVDVTIDASKTAANYWFNVTFSTGPCGASRIAKPAAIFQYDTATPGTPTSPGN
SPADPLCHDNVSYTPVISRTVPSGGFTPNDNNTIEVELLQKPWEDVPNRVYWNVHGHDMN
ITWENPTLEYVANGDLDFPERYNVHTVDKSNGDWAFWLIENTSVLPHPMHLHGHDFYVLG
RSDPPANPFNAPMTNFNPSTDMGRLRFSNPTRRDTTTMPARGWLLLAFRVDNPGAWLFHC
HIAWHAGQGLSMQFLESVADIPPTVDLSILEPVCSIWSDYYSTSQCKQWDSGL

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	57	360	1.1e-114	0.9743589743589743

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	4.55e-69	69	565	1	535	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	1.42e-68	67	191	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.
177843	PLN02191	1.96e-60	92	561	43	551	L-ascorbate oxidase
259968	CuRO_3_MaLCC_like	4.41e-59	381	555	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.
274556	laccase	4.40e-58	69	572	3	532	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
QBZ58298.1|AA1_3	2.07e-246	1	593	1	598
UQC90233.1|AA1_3	2.77e-220	1	593	1	605
AUS45857.1|AA1_3	1.37e-209	18	593	21	590
CDP29442.1|AA1_3	4.91e-208	10	593	27	621
VBB81234.1|AA1_3	6.95e-208	10	593	27	621

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PPS_A	7.68e-209	1	593	1	604	Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_B Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_C Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius],3PPS_D Crystal structure of an ascomycete fungal laccase from Thielavia arenaria [Canariomyces arenarius]
6F5K_A	1.87e-208	39	593	3	559	Crystal structure of laccase from Myceliophthora thermophila [Thermothelomyces thermophilus]
1GW0_A	3.75e-208	38	593	2	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]
2Q9O_A	5.31e-208	38	593	2	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]
3DKH_A	2.14e-207	38	592	2	558	L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces],3DKH_B L559A mutant of Melanocarpus albomyces laccase [Melanocarpus albomyces]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78722|LAC2_PODAS	2.48e-208	1	593	2	605	Laccase-2 OS=Podospora anserina OX=2587412 GN=LAC2 PE=2 SV=1
sp|Q70KY3|LAC1_MELAO	7.55e-208	31	593	45	609	Laccase-1 OS=Melanocarpus albomyces OX=204285 GN=LAC1 PE=1 SV=1
sp|Q03966|LAC1_CRYPA	1.03e-189	16	593	17	591	Laccase OS=Cryphonectria parasitica OX=5116 GN=LAC-1 PE=3 SV=1
sp|P06811|LAC1_NEUCR	6.01e-188	40	593	55	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|Q96WM9|LAC2_BOTFU	5.05e-135	1	593	1	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000346	0.999641	CS pos: 19-20. Pr: 0.9853

TMHMM  Annotations     

There is no transmembrane helices in jhhlp_003954-t41_1-p1.