CAZyme Information: FGRAMPH1_01T25365-p1

Basic Information

• Species: Fusarium graminearum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium graminearum
• CAZyme ID: FGRAMPH1_01T25365-p1
• CAZy Family: GT2|GT2
• CAZyme Description: laccase precursor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
677	HG970335|CGC29	77523.91	5.4288

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FgraminearumPH-1	14145	229533	2	14143

• Gene Location: location=HG970335:4175289-4177322(-)

Full Sequence      

MGETPFKWAKEDDPESPDSWSEEAEMSDTTVPRNETFVGRWMRLVVALLTVLSIFMLTAF
IFFQQSSFTHHQDSHSEHFQTTKPQATQASNSVEYKEDIPSIPQLRDTKEYILLQTWDFD
ASPTTREHFWTINQETLNPDGVYRPMLLINNQFPGPLVECNEGDTIIVHIKNDAPNATAI
HFHGMFQNGTNGMDGTVGVTQCPIAPNSTFTYKFDVRGQHGTYWYHAHHSAQASDGLLGP
MVVHSKKEHNLQKIDYATDRVVMVQDHYHNLTSELLMEYLAPDQENNEPVPDNGLINGRG
LRDCLDFRGWDCNSTDREMPNINLEAGQRHRLRIINVGAFAEFQVQFDEHPFYVTEVDGT
DVHPESVHRLNILPAQRYSVILETNATTGSAFWMRARMVTHCFKNENERLEPEAKAIIRY
EGHNKTSSNEKPTSKEWPDAIEVICRDLNTSSLRPVEVISPPPSDKVIILRANFEIGDWR
LARGFFNESTWHPNITSPSLHRFLDSGVQSTSKKTPIAINERVFDRNKELVLETTGIQTV
DISINNFDDGAHPFHLHGHKFFVLLQGRDGYPPSPAELPEYLEKHNLLENPLRRDVVTVE
GYAWAIIRVVLDNPGLWAFHCHNTWHAESGMVMQMLVRPEVMKDWKSTSEERDMCLRDGV
MSGMRPDDSLWFGQFNK

Enzyme Prediction     

No EC number prediction in FGRAMPH1_01T25365-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	136	631	2.7e-113	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.30e-69	125	631	1	517	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.
259953	CuRO_2_MCO_like_1	7.74e-68	260	421	1	163	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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.
215324	PLN02604	2.09e-67	125	631	24	540	oxidoreductase
259926	CuRO_1_Diphenol_Ox	7.07e-67	126	244	1	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which 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. 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	2.73e-63	121	631	19	540	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CEF85239.1|AA1	0.0	1	677	1	677
CZS73598.1|AA1	0.0	1	677	1	677
QPC73266.1|AA1	0.0	1	677	1	677
QPC64373.1|AA1	0.0	1	677	1	677
CEI39947.1|AA1	0.0	1	675	1	672

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.26e-75	110	636	51	541	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	3.40e-75	110	636	51	541	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]
1ZPU_A	9.50e-68	130	644	7	486	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
5LM8_A	1.86e-67	119	638	14	505	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.90e-67	119	638	15	506	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|J9VY90|LAC1_CRYNH	3.17e-99	85	655	21	578	Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1
sp|Q55P57|LAC1_CRYNB	3.39e-98	99	655	35	578	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	1.88e-95	99	655	35	578	Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2
sp|J5JH35|OPS5_BEAB2	7.77e-77	125	662	73	572	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|A0A067XMP2|PTAK_PESFW	5.21e-75	126	655	65	566	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999975	0.000020

TMHMM  Annotations     

Start	End
41	63