CAZyme Information: POW03035.1

Basic Information

• Species: Puccinia striiformis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
• CAZyme ID: POW03035.1
• CAZy Family: GH131
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
664		73440.98	7.1740

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93-210	15090	N/A	0	15090

• Gene Location: location=PKSL01000132:70297-73112(-)

Full Sequence      

MHELTSISAVSWEDGVTGVTQCPIPSNGGIYTYKFDTNGQLSFGPFDLSLTAKDCPRRPP
PPSMFLRTDCAFATWNKDSGLFVSFFVASFSLINSACDPQRRLHSGVSTKLTFLTPFVAV
FFYHCLAKPVVCDGNQGTSVMTHPWACKFLFSSHHQNLMADGINGPMIIHSPRDPLKRSI
DFDHDVVLMMADWYHNTSSDIVQEMLSEAGYFGTPAAPGANCALINGVGQWNCSLATTTQ
QCNQVTSPPGFTVTAGQRIRFRLINAGVHAMFFFSVDEHMLNITEADSTGIYGPSDFRHI
WLHNGQRYSVIVQTKEEDVDRNFYMRATMNSDCWAWVPNDIQDTALGILRLAHDDARPEN
VSKARPDTQGWPQDFPQECIDIDPSLMVPILKSTVPASVVGSGTFQAGFGFQLINNTAEH
LTREEAVRLAKEAHHDSSRDPNLRGKKKYVTISHRAKHYRDRSDGSAEDLHDVCRVPATF
HGKGGGYQENSSSRHAAVDTGQEKNRQHNPQRFGGRKSPAGITRLAGPPPTPAGTIGKYF
VNNVSWTTFPYQPVLHDLTPGGVGTINGSRVANVIFPTAEWYDLYLVNVDAAGSHPYHLH
AMDMHIVAYGRGFPTPEKLSKIKYSTENPLRRDTVVVPSASFVVVRLNADIPGAWIMVLL
IRIL

Enzyme Prediction     

No EC number prediction in POW03035.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	148	657	5.8e-48	0.7178770949720671

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259950	CuRO_2_Diphenol_Ox	4.47e-82	186	350	1	162	The second 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 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. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Laccase is a multicopper oxidase (MCO) 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.
259971	CuRO_3_Diphenol_Ox	4.52e-63	526	657	1	140	The third 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 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.
259953	CuRO_2_MCO_like_1	2.37e-37	186	350	1	161	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.
259868	CuRO_2_LCC_like	3.59e-27	186	350	1	151	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.
259947	CuRO_2_MaLCC_like	2.10e-26	187	364	3	162	The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. 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. It 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. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV98963.1|AA1	1.09e-79	149	657	135	525
QRW13512.1|AA1	2.96e-79	149	657	135	525
QRV98945.1|AA1	8.10e-78	149	657	165	555
QRW13493.1|AA1	4.42e-75	149	657	165	555
QRV82887.1|AA1	5.31e-74	149	657	148	528

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6H5Y_A	9.58e-21	149	331	106	264	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]
5ANH_A	1.28e-20	149	369	106	297	Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1]
5A7E_A	4.01e-20	149	368	106	296	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
4A2D_A	3.94e-19	149	368	106	296	Coriolopsis gallica Laccase T2 Copper Depleted at pH 4.5 [Coriolopsis gallica],4A2E_A Crystal Structure of a Coriolopsis gallica Laccase at 1.7 A Resolution pH 5.5 [Coriolopsis gallica],4A2G_A Coriolopsis gallica laccase collected at 8.98 keV [Coriolopsis gallica],4A2H_A Crystal Structure of Laccase from Coriolopsis gallica pH 7.0 [Coriolopsis gallica]
4A2F_A	3.96e-19	149	368	106	296	Coriolopsis gallica laccase collected at 12.65 keV [Coriolopsis gallica]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	1.47e-47	149	655	159	540	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|J9VY90|LAC1_CRYNH	1.77e-45	149	655	159	540	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	1.16e-42	149	655	159	540	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|Q01679|LAC1_PHLRA	5.63e-20	149	327	127	283	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2
sp|Q12542|LAC2_AGABI	7.08e-18	149	350	124	308	Laccase-2 OS=Agaricus bisporus OX=5341 GN=lcc2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000055	0.000004

TMHMM  Annotations     

There is no transmembrane helices in POW03035.1.