CAZyme Information: HMPREF1541_02772-t46_1-p1

Basic Information

• Species: Cyphellophora europaea
• Lineage: Ascomycota; Eurotiomycetes; ; Cyphellophoraceae; Cyphellophora; Cyphellophora europaea
• CAZyme ID: HMPREF1541_02772-t46_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
705	KB822718|CGC24	72243.69	5.3957

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CeuropaeaCBS101466	11153	1220924	59	11094

• Gene Location: location=KB822718:3329804-3331921(+)

Full Sequence      

MSSFKATCLSLLALASIATATPAAVSQAAPSASPSASSCSSSKCQSFTIDLTWGKTDGAN
SFSRNAILTNGSFPGPPLKLKQGDCVDFTVINNMEASTAVHFHGIRQLATPWSDGVPGVS
QTSIKGGDSYTYNWIADEPGAYFYHSHYKGQMMDGLYGAIIISPAENATLPFSSLGDDKA
VKQITAANENIETILVSDWSRFTFDELFGYEQAANIDAACTDAFVLNGKGSQYCPDAAFL
AAQSAPPAAKILNGTSLTAKGCIPASNAQVQGPQYNRTLSALPPGAYDVCTPSTGKNYTY
TVDAASGWAAISFMSPAGTALFKISIDGHQMYVYSINGQYIAPQKVDQIGLDNGDRVTVL
VKLDQPAADYTIRVANAGLNQVISGFGTLSYKGSKGPAAVAPSMSYGGGNATAIVPLNRA
AGAPVGNVSPPVAAQADKTFMLDIMKAPSVPAAWEWVLNGDEPYNQTLDDATTPLLYQNP
SAIPESDLILRTNYNEWVDLIIIVKGPLAQPHPIHKHANKFYVIGAGTGDFNYTSVAAAQ
AAGVPFNLQNPPYVDGATTPPAEGKSAWLALRYKADTPGAWLLHCHVQTHMSGGMAVAIL
DGVDKFPTVPKDAGKTCGIDGNGSGSGKDNNGSGSGSGSGSGSGSGSGSGSGSGSGSGSG
SGSGSKGGSGNGTEPFTGAAAPNAGSAGVMFAFAAVMVAAAMNVL

Enzyme Prediction     

No EC number prediction in HMPREF1541_02772-t46_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	61	596	1.5e-73	0.9832402234636871

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.26e-72	437	602	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	4.55e-68	66	618	22	539	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	8.75e-63	62	610	41	555	oxidoreductase
177843	PLN02191	1.49e-60	70	619	48	563	L-ascorbate oxidase
259919	CuRO_1_Abr2_like	8.28e-56	47	162	1	116	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIW00656.1|AA1	8.75e-172	47	620	40	619
UQC89926.1|AA1	6.41e-162	47	610	41	612
QRC97610.1|AA1	4.35e-161	47	611	42	612
UJO20936.1|AA1	3.61e-158	47	612	26	603
QBZ54343.1|AA1	5.20e-154	47	610	30	601

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	7.20e-44	70	618	28	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	2.23e-40	60	601	82	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	5.53e-40	60	601	82	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]
5LM8_A	2.31e-39	47	608	28	511	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.34e-39	47	608	29	512	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|Q0UHZ8|ELCG_PHANO	7.73e-162	47	611	42	612	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	1.77e-151	47	610	50	621	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	2.13e-132	47	612	22	582	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	6.03e-119	45	610	26	589	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	1.70e-114	51	614	31	601	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000218	0.999758	CS pos: 20-21. Pr: 0.9876

TMHMM  Annotations     

There is no transmembrane helices in HMPREF1541_02772-t46_1-p1.