CAZyme Information: KAA8897973.1

Basic Information

• Species: Diutina rugosa
• Lineage: Ascomycota; Saccharomycetes; ; NA; Diutina; Diutina rugosa
• CAZyme ID: KAA8897973.1
• CAZy Family: CBM21
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
607		68836.31	4.5162

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_DrugosaCBS613	5819	N/A	4	5815

• Gene Location: location=SWFT01000149:181446-183269(-)

Full Sequence      

MLLLWLLIGYVWAKTHTYNFNVSWVDADPDGQGTRLMIGVNGQFPPPPIRVKPRDRVIID
VHNGLGNKNTSLHFHGLFMHGQNSMDGPEMVTQCPIVPGQNFTYNFTVDDQTGLYWYHSH
SGSQYADGLRGLFIIEDEDYGFDFDEEMVLSLSEHYPKSSGAIMQEFLSRYNPTGAEPIP
RNSLFNETKNVTWHVQPDTTYLLRIVNMGLFTSQHFVIEDHQLTIVEIDGVKVEPYTVDS
LYITVAQRYSVLVTTKKSTKKNFRMLNVIDMPMLDVIPRDLQIISTNYVVYDDKASLPAP
AVNTKTSFDEYVERYPYFDDSVLVTRSRRELLGDPDYRINLNFTMDHLGDGVVYAFFNNE
TYVTPKVPTLYSVVSSGKYAGDSLVYGTNTNTFILQKDEVVEIVLNNMDPGKHPFHMHGH
IFQLIARSEEGEEDDPIIYDPENSNVTFPEYPMMRDTVEVQPNGYMVLRFTADNPGVWFF
HCHVDWHLEQGLAITLVESPFDIQRQDIPGDHFAACEAANVSYYGNAANHSGDTKQAWLN
LDGQNSQKPPLPAGFTFKGYAAFAACAAAAIYGLISIYQYGIEDVTTVETEEMVTKLYQL
IDTDSNE

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	35	378	9.4e-145	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	3.39e-85	13	501	33	451	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
259966	CuRO_3_Fet3p	3.22e-79	336	500	1	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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	2.60e-74	18	498	4	523	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.
259945	CuRO_2_Fet3p_like	1.34e-69	146	293	1	148	The second Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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.
259920	CuRO_1_Fet3p	1.05e-66	16	135	1	120	The first Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p 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
ABN68144.2|AA1_2	9.27e-281	1	603	1	612
CAG88101.1|AA1_2	6.42e-264	13	602	18	610
QEL59042.1|AA1_2	4.17e-260	13	601	20	617
QEO20037.1|AA1_2	4.17e-260	13	601	20	617
QRG36491.1|AA1_2	1.19e-259	13	601	20	617

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	3.86e-195	14	554	1	534	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]
3KW7_A	2.85e-68	19	502	7	476	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
1V10_A	1.29e-64	13	498	21	489	Chain A, Laccase [Rigidoporus microporus]
2QT6_A	8.01e-62	29	509	17	480	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
1GYC_A	1.59e-61	29	504	17	475	Chain A, LACCASE 2 [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	4.35e-221	13	589	21	586	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	4.66e-207	13	591	25	597	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|P38993|FET3_YEAST	3.81e-202	3	598	11	598	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	9.39e-195	11	593	15	594	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1
sp|E9R598|FETC_ASPFU	4.69e-192	13	586	20	577	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000383	0.999573	CS pos: 13-14. Pr: 0.9792

TMHMM  Annotations     

Start	End
560	582