CAZyme Information: ASPSYDRAFT_91522-t33_1-p1

Basic Information

• Species: Aspergillus sydowii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii
• CAZyme ID: ASPSYDRAFT_91522-t33_1-p1
• CAZy Family: GT34
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
590	KV878589|CGC1	65481.53	6.5316

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsydowiiCBS593.65	13717	1036612	138	13579

• Gene Location: location=KV878589:1167661-1169536(+)

Full Sequence      

MKTSLLSLLALVARSVATPAPRANVRDISIQHSAGTKPCKNTPTSRHCWGKYNIDTNYYT
TTPDSGRTIEYWLSVEEGTCNQDGYVRPCMTFNGTMPGPPIIANWGDKLVVHVANNMKTN
GTAVHWHGARLHHSNEWDGVPGVTQCPIAPGESLTYKFRVTQYGTSWYHSHFSLQSTEGL
FGSLIFNGPATANYDEDLGPIFLQDWSHIPTFTAWEAKQKWGITHSQTTTLINGINTFNC
SASLDPNCVGGGKKFEAVFKPGKKYRLRLINVAMDSQWRFSIDGHKLQVIANDFVPIEPY
ETDSVLINVGQRYDVIVEANATPGDYWLRGGWVKSCQGVANEHPDSATGIIRYDHSSISD
PTSTTTIEAPKSCDDEPQKNLVPHLKLDVGTIADTTVEDINVRLTNAAVFQWTVNSSSLV
LDWNEPTLKRVFDNASIFPTPYNVVEVDKKNPHGDEWAVLVIENKAAAFFGGIAHPIHFH
GHDVWIVAQEKTPWDGTTASFQTINPPRRDTAMLPPHGYLALAFQLDNPGAWLVHCHIPW
HASMGLALEFVESQGSISIKKAHRKAFDETCKKWSQWSEGAPYPQDDSGI

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	56	373	3.6e-129	0.9935897435897436

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	9.18e-73	83	552	16	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.
177843	PLN02191	2.02e-71	65	552	20	546	L-ascorbate oxidase
259947	CuRO_2_MaLCC_like	1.19e-66	198	366	1	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.
215324	PLN02604	9.87e-66	83	552	39	546	oxidoreductase
259968	CuRO_3_MaLCC_like	1.10e-63	399	551	13	157	The third 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 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABM21605.1|AA1_3	6.32e-241	36	590	40	584
AFC76164.1|AA1_3|1.10.3.2	5.58e-236	7	590	9	580
QBZ63059.1|AA1_3	4.11e-235	9	590	11	597
ATZ57071.1|AA1_3	6.25e-233	7	590	9	581
AAK77953.1|AA1_3	6.25e-233	7	590	9	581

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	1.93e-237	7	590	9	580	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
3V9E_A	3.87e-237	7	590	9	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LWX_A	5.58e-139	15	583	11	562	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	2.09e-137	41	583	1	534	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.15e-137	41	583	2	535	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96WM9|LAC2_BOTFU	1.11e-233	7	590	9	581	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	9.11e-198	1	590	1	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|J5JH35|OPS5_BEAB2	4.33e-185	3	590	11	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	5.27e-131	39	590	28	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.69e-127	39	590	26	610	Oxidoreductase ptaE OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaE PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000311	0.999670	CS pos: 26-27. Pr: 0.4490

TMHMM  Annotations     

There is no transmembrane helices in ASPSYDRAFT_91522-t33_1-p1.