CAZyme Information: KFA46114.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA46114.1
• CAZy Family: AA3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
623	KL651667|CGC1	69501.27	4.4336

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SchartarumIBT40293	11453	1280524	0	11453

• Gene Location: location=KL651667:196022-198018(+)

Full Sequence      

MASRFTSLLRAVSALPFALGVLAQPYGPRKEFGLDVTWGQYSPVGGASRDMFMMNGQTPG
PTIEVDQDDWVVVRVQNDSPFNITIHFHGIEMYGTPWSDGVPGVTQRPIRPGDSFVHEFK
ATQHGSYWYHAHYRGHIEDGFMGPIVIHPRRGDPKPFSMISDDPQAVLAMEAAEMQVRPL
LVTDWMHLTSDDKWAITVDAALEMPCYDAILFNGKGRVQCLTEEQIEAHISQGQRDNLDL
VEGSTFTDKGCLPPDVMGLVLGDPEIPINTSVIPEHVFYGCNPTDAEIEVITVPEATGAE
RWVAIDLIAGMNFIRSAASIDEHDMWVYAMDGSYIEPQRVQAIRMASGERYSVLVKTDEP
GDFRIRVNSVSVPQMLTGYALLSVDGPSKRQDGAGNDDESGAFIDIVGTPAQEDVEFFDQ
THAAPFPPQEIPQSADELYIVNMRGDGATYLWALNNSRLMPADFEDEAPILMDTPHIRDN
VTLTTRNGTWIDLVFMAARFPLPPHPIHKHGNKMYYLGSGTGRFRWASLDDAMEEEPQNF
NLRNPPQRDTFDTPQARGEITWMVVRYEVSNPGPWMLHCHISNHMMGGMSMVIQDGVDAW
PEVPAQYRLDTIEEQRYSVGGGV

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	47	246	1.4e-51	0.5139664804469274
AA1	304	589	4.8e-28	0.4888268156424581

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	4.49e-74	436	596	1	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	7.86e-61	54	606	25	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	2.11e-58	54	605	48	556	oxidoreductase
259919	CuRO_1_Abr2_like	5.74e-55	34	148	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.
177843	PLN02191	1.58e-53	54	604	47	555	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPL02374.1|AA1	1.69e-242	30	607	32	600
UKZ96290.1|AA1	3.44e-234	30	607	26	598
ATY64049.1|AA1	1.09e-232	25	607	30	608
QYS99552.1|AA1	2.04e-232	8	607	10	605
QUC23423.1|AA1	1.17e-231	12	607	7	597

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	7.87e-42	54	606	27	534	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	7.30e-39	25	591	63	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.83e-38	25	591	63	538	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]
5LM8_A	4.22e-36	30	593	24	502	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	4.27e-36	30	593	25	503	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9RBR0|ABR2_ASPFU	4.50e-143	19	605	9	581	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|E9F648|MLAC1_METRA	1.41e-139	34	609	27	612	Laccase 1 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=Mlac1 PE=2 SV=2
sp|A0A0B4F5S2|MLAC1_METBS	1.99e-139	34	609	27	612	Laccase 1 OS=Metarhizium brunneum (strain ARSEF 3297) OX=1276141 GN=Mlac1 PE=3 SV=1
sp|A0A0B4HQH6|MLAC1_METMF	4.09e-139	3	609	2	613	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1
sp|A0A0B4F1I0|MLAC1_METAF	1.53e-138	34	608	27	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 SP

Other	SP_Sec_SPI	CS Position
0.000308	0.999646	CS pos: 23-24. Pr: 0.9773

TMHMM  Annotations     

There is no transmembrane helices in KFA46114.1.