CAZyme Information: EEU34620.1

Basic Information

• Species: Fusarium vanettenii
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
• CAZyme ID: EEU34620.1
• CAZy Family: PL3
• CAZyme Description: Plastocyanin-like domain-containing protein [Source:UniProtKB/TrEMBL;Acc:C7ZMZ6]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
397	GG698960|CGC2	43681.80	6.3855

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fvanettenii77134	15708	660122	0	15708

• Gene Location: location=GG698960:47186-48692(-)

Full Sequence      

MKAEGSKYYCYDSILVNGKGRVHCRQLDFAHLNGNALDGKGCIQPAGLPNEYCSPTSADY
EVFETGGQRYVMMNLRNNGFEHSVKVSIDGHQMVFVANNGGFVVPEQTDVVYIPSAARIP
ILVKLDAEPEGKADSINIKAKRLPRYGEPMVLPAPASPKDVCLLADTSTKPHCKTTDGQF
VPPFPSKPPPASDKKHPERADFTFRLSAGSQPSLTEPKVPEFNLNEKPWQLFHGSMTPLL
FHRLGRDEELDKPIISGMPVGSVVDLIIENQINDTIRLYKHGDPAWLLGSSSGQPFREES
VEDAIIAAGNSHTSLNLHNPALVTVHDLPPLGWSVLRFQVTSKAANMLHSAKLRNFLLGM
TVPILEGIRAENPIEIPEEVLDRPHVQFEPKNDGIFG

Enzyme Prediction     

No EC number prediction in EEU34620.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259944	CuRO_2_Abr2_like	1.57e-30	1	129	20	113	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.
259965	CuRO_3_Abr2_like	2.49e-16	221	367	16	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.
177843	PLN02191	1.85e-11	13	381	189	559	L-ascorbate oxidase
259960	CuRO_3_AAO	5.02e-08	253	368	33	148	The third cupredoxin domain of plant Ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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.
259868	CuRO_2_LCC_like	3.13e-07	10	130	30	125	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CEI62062.1|AA1	3.55e-185	1	397	234	641
QPC59569.1|AA1	2.67e-182	1	397	234	641
QPC70978.1|AA1	1.52e-181	1	397	234	641
CEF78326.1|AA1	2.00e-179	1	397	234	641
CZS81621.1|AA1	4.02e-179	1	397	234	641

PDB Hits     

EEU34620.1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	4.22e-37	9	390	198	584	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	3.40e-17	9	385	197	610	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	1.11e-16	2	368	198	590	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	6.42e-15	9	368	194	587	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|P17489|LAC1_EMENI	1.41e-13	4	368	193	604	Laccase-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=yA PE=2 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000017	0.000021

TMHMM  Annotations     

There is no transmembrane helices in EEU34620.1.