CAZyme Information: jhhlp_006328-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_006328-t41_1-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
626		69244.64	5.9899

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=NLAX01000701:3441816-3443815(-)

Full Sequence      

MNYLPVTTNYNLHLLVRSHEMLCSVVYRLLIGLAFFTVVLGQATRTFKLSLTLGNWSPNG
HQRQVILVNGQFPGPTLKMWQGENVVVEVENNITNATSIHFHGIEMHDTPWSDGAPGVSQ
RHIQPGKSFTYRWMATQHGSYWYHSHSRHQIEDGLFGALVIAPKPDTPKPFDKISTASRA
IKTMESADESANILLLSDYRNMTGDEAWELTQKAELDPACWDSILINGKGRVHCPEPAEI
DALLSDLQRTQLGKMNATMTSKGCYPPQLMALAWNGHGNGSVVPSHVFDECQSTEGWREI
LSVDHKSTCDDESWIAIHFIGAFQSITATVSVDEHPMWVYAADGGYVEPREVQAITITNG
ERYSVLIKANKAGKFNIRVASINDPQIIAGYATLDVKIAGSEGNGHESVPYINDAGMAIS
SGVVIFDQSFVKPFPPVAIPQTVSATHVLEMGNIEPAYIWTMNSMPLESLTLEQQTPFLL
NPQLTTNLTIPTQNNTWVDLILVTHVSPNPAHPIHKHGVKMHLLGTGYGPWVWSSVEDAA
RQMPSSFNLVDPPLKDSFTSLRVGLEAGQEVAWMALRYHSRNPGAWLLHCHVLQHLVGGM
QVVLLDGVDVWPEMPEEYRALAEGSG

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	61	601	1.7e-77	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	2.73e-66	446	607	3	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.
274555	ascorbase	1.48e-54	44	617	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.
215324	PLN02604	3.05e-53	29	626	10	566	oxidoreductase
259944	CuRO_2_Abr2_like	7.87e-51	194	397	3	138	The second 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 2 of 3-domain MCOs has lost the ability to bind copper.
177843	PLN02191	1.55e-49	25	617	4	557	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL02374.1|AA1	3.46e-184	34	625	17	607
QKD54095.1|AA1	4.28e-183	44	624	30	606
QGI95094.1|AA1	9.76e-182	44	624	30	606
QGI81474.1|AA1	9.76e-182	44	624	30	606
QGI64209.1|AA1	9.76e-182	44	624	30	606

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.93e-43	45	624	4	539	Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
3V9E_A	2.15e-37	44	606	67	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	5.35e-37	44	606	67	542	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]
5LWX_A	2.16e-34	59	622	66	570	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	2.22e-34	59	622	38	542	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9RBR0|ABR2_ASPFU	3.92e-139	30	614	8	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|Q0UHZ8|ELCG_PHANO	2.51e-128	47	618	42	614	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	1.31e-125	46	624	25	598	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|E9F648|MLAC1_METRA	1.94e-124	28	619	6	611	Laccase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=Mlac1 PE=2 SV=2
sp|A0A0B4F1I0|MLAC1_METAF	3.75e-124	28	619	6	611	Laccase 1 OS=Metarhizium anisopliae (strain ARSEF 549) OX=1276135 GN=Mlac1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000003	0.000016

TMHMM  Annotations     

Start	End
21	43