CAZyme Information: KIS66366.1

Basic Information

• Species: Ustilago maydis
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
• CAZyme ID: KIS66366.1
• CAZy Family: AA6
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1288	CM003158|CGC2	135811.95	4.9411

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Umaydis521	6910	237631	145	6765

• Gene Location: location=CM003158:320283-324149(-)

Full Sequence      

MRITHAFMERGGRYRRLLSIGLAWVALILVLFVLLTASLSAAVPVSTTAERTEGTGNEAQ
SHFDGEEIDHRKLLRKRHEQISSGSVATGFAHPTHLYRRDADALPPPDKAYNMSVTQGII
SPDGFERLGFLMNGNFPADPFVWDENDDVEINVINNGPVPFAIHWHGIHQIGSPEMDGVP
GLSQWNIYPGESYTYRFKLVNQYGGYWYHSHERGYYADGLRGTIYIRPKPGRQKPWSYIS
TDQDDIEQMEAAEHDSQIMSLSDHWHINHTEMLLVVHETGVPPACFDSLHINGRGRQYCV
NNWSKVISPIQASLLRNFSSTNPEGITSKGCISLVPPKSGYTVKGTLDERYGGVCQNTTA
PLTVFSAAKAIKKGRRWLNLQVVDTATNWYYGISVDSHKMWIVAVDGHYIQPMQVDWAQI
TIGSRLSVMIQLDPALDGNMFPIRLTGARALQPIEGHAFLSYIDDVDGTWNPGQEEDFGY
LMRTLTTAHVPMSGFVSDPSVVKWKQNLSVPFDPINQVPQTSNMTLHAVASQNSLNVWQV
ATMPLDTARLADDRPILFNATDGNATLNQMTPYASIPFGTVVDVIMENNIYSIVGGPNSP
HPFHMHSRRFWIIGSGAGPFPADTVAEAQGQGILFNLETPPLRDGFDIDSNSWVVIRYVA
DHAAANILHCHIDDHAIEGMAAVLLEGLEKIPAGGNFSDTIKARPSKWVETKNDELGQVL
EASWATGSANAKYVAPAPTDTVDPWGDPRSLAQSIQLYASSNSVLKAITSSLVSEMGEVK
ATATGVVTAITATVSDHLTTFTGVAASSSVFATTTASVTLATVTENAVASASSTAIVATA
TESASASVASAQSLAAVASTTTALTLAVETLTSVLSVSASQVINTVVSATDTSAAAVATS
NTVTSINTAQSTLFAIAFTTEVVTASAAETPTVKSSVETPAIITSSSTVYVTVLATVAPT
LSLSSLAAQSTKSSSSAAIKTTNASSTRVSLASQTTVAAVSTASLVSLLPYTTLYATVPA
STALFSTGTSTLLKLDGQTAAATTTKTATSPSLSTQSASRTDADSGIEDDDVVTEETDNI
GASATTSLSSQSMSSSASLRVASANLVLTTSVVAADSTSTAQASSTVVIERAGTTTIASL
NRAASTHVSASTTSARAVLTEVATTSATQTPHTTISESQASRATSQSTSTGSEAASPTAN
AANYGTHSAATTFLAYSTSVETSEAALTSSSATVSEDEPAYDNPVFPSSTGAVSTSTTTA
ATKPTNSFTSSGTGNEGESGGYDTQADG

Enzyme Prediction     

No EC number prediction in KIS66366.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	125	681	1e-69	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259919	CuRO_1_Abr2_like	3.87e-67	111	227	1	117	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.
259965	CuRO_3_Abr2_like	2.78e-56	519	687	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	7.68e-53	121	691	14	528	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.
259944	CuRO_2_Abr2_like	5.05e-47	257	462	1	137	The second 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 2 of 3-domain MCOs has lost the ability to bind copper.
215324	PLN02604	9.13e-46	121	691	37	551	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS81959.1|AA1	0.0	5	810	5	809
SJX65792.1|AA1	0.0	1	810	1	811
CBQ70142.1|AA1	0.0	1	810	1	811
CDI56165.1|AA1	0.0	13	809	13	810
SAM85614.1|AA1	0.0	31	812	8	789

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.64e-37	111	691	6	528	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]
2HRG_A	1.66e-33	112	693	7	473	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
4JHU_A	1.66e-33	112	693	7	473	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
3V9E_A	6.20e-33	109	691	68	547	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
6H5Y_A	7.22e-33	112	693	7	473	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X732|PFMAY_PESFW	1.46e-86	109	693	23	572	Laccase PFICI_06862 OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PFICI_06862 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	1.34e-75	111	692	22	577	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	1.21e-74	121	692	32	591	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	2.77e-71	113	692	28	586	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	9.95e-71	121	692	37	594	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 OTHER

Other	SP_Sec_SPI	CS Position
0.999925	0.000101

TMHMM  Annotations     

Start	End
20	42