CAZyme Information: KNZ43953.1

Basic Information

• Species: Puccinia sorghi
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia sorghi
• CAZyme ID: KNZ43953.1
• CAZy Family: AA1
• CAZyme Description: uncharacterized protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
753		83200.59	7.3401

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=LAVV01015358:13913-17370(-)

Full Sequence      

MHQKRARRGCIIFFLNALLLVSIVASVKLNSSELYLSDKFEITSTPQTRNYYWSITADLS
FRNETAAPDGFTRNMLVVNSQFPGPLIEANVIFSAAIFACATNLDVLNHFSLHFMSPSRR
GQFNDTLNILVVNKISAGVTIHWHGVIFPKGNSLDGWGGTIFSTGVTQCQIQPGRNFTYT
FNIGKQYGTFCMYPIRKPIKKKRMDGHSLKVSSLSFRVSRPRAEFEFGRNRPMIVHSVND
PLKRGVDYDQDIILLVNMSERILGQLLSPTGYNNIILDFSSFFLSCAGKYDEHEYSSANS
ALVNGIGYFDCNNAPANASCTTPTNSLSFDIPVRTKTRFRLIQAGSHAMFRFSVDEHTLN
VTEADSTGVAGPTAIHRVPFHNGERYSVIIDTSQDTVGSTFYLRAAMDTDCCMWNDFMFA
KSSCPVTNFLQITALGFGDQVAWLAPGITGRASTALGIIRVIDPNNPPHANSDPALPTTR
DWLDALGGACLDLDVSTMRPLVPQDACTNLLRTVYFSTSFGTITSVEGNSSAVSGRFFVN
GTTWITRPNRPLLNELLYGGPGTINASDVAAFTFEQVGCYDIVINNLDAALDHSYHLRKK
SMDLLIIHDSIYLSHSSFVPSQGWIVATGTGEINATTVSSLTYNTTNPLRKDVSEKSLES
YSSCGRWELSCRLVVRVLADNPGVWILHCHLGWHLGAGFAGMFVMQPSVLRNMTSPEGNQ
ELCRAISPEDIDEIEPGKRRRSLLPYALSDLKI

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	291	699	8.4e-26	0.5921787709497207

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259950	CuRO_2_Diphenol_Ox	6.44e-63	257	416	11	152	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	1.46e-60	513	705	1	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.
259926	CuRO_1_Diphenol_Ox	1.37e-31	49	190	1	98	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.
259953	CuRO_2_MCO_like_1	1.99e-30	299	411	33	144	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.
259869	CuRO_1_LCC_like	1.02e-24	49	193	1	101	Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They 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 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV98945.1|AA1	2.44e-116	32	743	51	610
QRW13493.1|AA1	3.42e-116	32	743	51	610
QRV91744.1|AA1	3.76e-112	40	743	39	578
QRV76916.1|AA1	3.76e-112	40	743	39	578
QRW05810.1|AA1	9.26e-109	40	743	39	578

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JHU_A	8.35e-29	58	730	7	495	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
6H5Y_A	3.60e-28	57	730	6	495	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]
5A7E_A	2.08e-27	57	730	6	495	Chain A, CORIOLOPSIS GALLICA LACCASE [Coriolopsis gallica]
5ANH_A	3.72e-27	57	730	6	495	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]
2QT6_A	9.08e-27	57	723	6	487	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	1.49e-81	25	745	38	595	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|J9VQZ4|LAC2_CRYNH	1.47e-79	25	743	38	593	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	1.11e-78	25	742	38	594	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|S8FGV1|LAC2_FOMPI	5.99e-28	59	723	32	520	Laccase-2 OS=Fomitopsis pinicola (strain FP-58527) OX=743788 GN=LCC2 PE=1 SV=1
sp|Q99044|LAC1_TRAVI	9.99e-27	57	730	27	519	Laccase-1 OS=Trametes villosa OX=47662 GN=LCC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.240774	0.759190	CS pos: 26-27. Pr: 0.6189

TMHMM  Annotations     

Start	End
9	27