CAZyme Information: KNZ56187.1

Basic Information

• Species: Puccinia sorghi
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia sorghi
• CAZyme ID: KNZ56187.1
• CAZy Family: GH38
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
759		84316.34	8.9705

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsorghiRO10H11247	21769	N/A	691	21078

• Gene Location: location=LAVV01007362:4371-8116(-)

Full Sequence      

MAIKQTCGMDLRASRVQSYKTTMTTVTSWSVNATLSGSSQNYTNNPILPHVDAGTVQVNS
PSLVLKKDHIITNVPQVRRYDWVVANRTASFDGFVRNVFVINNQFPGPLIEVRFFPFFGD
TIVVTVKNELNVPLTIHWHGKNKPVPSYVHMNRRNLTENPFYNSGIFQRGSQWVSSVVPW
LRWTGSPGLLSVHNSLALHSLTNSLSQTSLELFAHYSALLADGISGPLIIHSLNDPLRLV
PRVTQAPPSRANCYQRKDTMGVSPPLPQTRVCISNYLVNEKASEEISILFFFLLFFPKAL
LNGVGFFNCEKYAKGQPCRTNSNRLEIQVPPNERSRLRLIQAGAHALFKVSVDGHPLEVI
EADATPVQSSVLFHRVPLHNAERYSVILDTSSDSEGDSFYLRAAMDTDCCKTFFYLFKIA
PGMDTTEGNTALAIVRVSSTPLANGNARARMALPSTKDWQDDLDGPCIDLDQSKISPRIN
PNLNSTSLGRVRYIFDNIRASILKKVYFNTSFGTIIDHSVPKGARNVFGRFFVDNTTWIC
LLDFQFREKKLARLINTYFLLSPPARETQPLLPQFLNGGSGALNTSEVATQTISQPGIWD
VVINNLDQAIDHPIHLREAYSSTSLKYKSHPTQKTFPTCVETCLVASGNGTLSETNQSTA
QYQLGNPVCRDVHVVPGGTYAVSESPKILVGSNFRCDKYHLIPGMRINANNPGVWILHCH
IDWHLAAGFAGMLVIQPNVLKQTVLPQANLDLCPKGGYK

Enzyme Prediction     

No EC number prediction in KNZ56187.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	214	729	1.1e-31	0.7374301675977654

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259971	CuRO_3_Diphenol_Ox	2.37e-61	506	735	2	158	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.
259950	CuRO_2_Diphenol_Ox	9.89e-49	302	438	41	164	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.
259953	CuRO_2_MCO_like_1	1.24e-29	302	436	38	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.
259926	CuRO_1_Diphenol_Ox	1.36e-27	78	231	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.
259923	CuRO_1_MaLCC_like	4.65e-19	76	231	2	122	The first 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. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV98945.1|AA1	6.67e-90	63	753	53	591
QRW13493.1|AA1	3.54e-89	63	753	53	591
QRV91744.1|AA1	1.90e-84	68	753	38	559
QRV76916.1|AA1	1.90e-84	68	753	38	559
QRW05810.1|AA1	2.89e-80	68	753	38	559

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5NQ7_A	3.09e-18	81	754	28	508	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
5LM8_A	4.65e-18	72	734	20	503	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	4.66e-18	72	734	21	504	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
3DIV_A	4.99e-18	81	754	7	489	Crystal structure of laccase from Cerrena maxima at 1.76A resolution [Cerrena]
4JHU_A	6.52e-18	81	754	7	486	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	4.13e-66	51	753	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|Q55P57|LAC1_CRYNB	2.01e-65	50	753	34	578	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	1.84e-63	50	753	34	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|A0A067XMP2|PTAK_PESFW	3.82e-25	77	753	64	566	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|S8FGV1|LAC2_FOMPI	1.37e-19	84	754	34	521	Laccase-2 OS=Fomitopsis pinicola (strain FP-58527) OX=743788 GN=LCC2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000009

TMHMM  Annotations     

There is no transmembrane helices in KNZ56187.1.