CAZyme Information: KIW07853.1

Basic Information

• Species: Verruconis gallopava
• Lineage: Ascomycota; Dothideomycetes; ; Sympoventuriaceae; Verruconis; Verruconis gallopava
• CAZyme ID: KIW07853.1
• CAZy Family: GT24
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
819		87506.11	4.2802

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_VgallopavaCBS43764	9871	N/A	53	9818

• Gene Location: location=KN847532:916167-918785(+)

Full Sequence      

MAAITRYAFALSSLSFLSSVRAVPFPGNDDTCVRTTTTVYTTVTVGEGWEQTTSVANAAA
ASTATTSAAEGSWAATDSVEAVTQQYTPPSDFTYPGVTFPTFSPSSLNPNGPFYNPNDFI
PYYVDWPGKPSSGASTPPPLPTKAPKPSGGYSASEYKSPAWQQVGKDLTPGLSQEETNGD
SQWGLIDCPRLSSYLGSGYSASSSKSGSGSYYTSAVSSSYVSGVHYTSAAYSAYPTYSAS
SNGTKSTTSFSLVTSSSSSSASPSSSAPSCSANNTAAFCASKMPDTGVTRTYEFTVAYAT
IAPDGVQKNGLVVNNQFPGPLIEANWGDWIQVTVTNDLPEYSQEQGEGTSLHWHGFLQQE
TPYYDGVPSVQQCPIAPGKSVTYTYRADHIGTSWYHSHYSSQYAGGALGPVVVHGPQIPG
ACYDEDLGPVFINDWYHADYYSLVETTMAGGLPLSDNILINGKMNYPCDNTTAVCTANAG
ISKFQFTPGKKYRMRLINPSAEAILKFHIDGHNLTVIANDFVPIVPYTTNVVTVGVGQRS
DIIVEATGSAGDSYWMRATGGNALAGTGCALTSGVVTEGVAAVYYDGADTDSEPTSTSDA
TSDQLLRCQNDDLSLTRALCPIALDDDADVFTQTITMEFASNGTNFVWFMNNSTFHADYN
VNLLDQIIGGNTTFESDWNVYTFDSSKSSIRIIFENTFAFPHPMHLHGHDFNVLADGVGT
WDGTIVNPSDTQARDVHYLPGATSDGNGYAVIQFKMDNPGLWPLHCHIAWHVSAGLYVNI
LERPDAITYQVPSALEQTCVDWAAWEAAGNVPDQIDSGL

Enzyme Prediction     

EC	1.10.3.2:2	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	281	602	7.6e-116	0.9711538461538461

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	6.57e-66	287	414	1	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.
259968	CuRO_3_MaLCC_like	2.40e-60	629	781	6	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.
259947	CuRO_2_MaLCC_like	3.05e-60	427	603	1	167	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	2.02e-56	289	778	24	542	oxidoreductase
274555	ascorbase	1.45e-55	289	778	1	519	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDS68790.1|AA1_3	2.28e-264	3	819	2	799
CAE7013418.1|AA1_3	7.50e-209	111	819	52	737
USW51556.1|AA1_3	1.74e-207	149	819	59	665
UJO18649.1|AA1_3	2.00e-203	147	819	77	685
QDS70373.1|AA1_3	5.01e-199	283	819	164	698

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3SQR_A	2.89e-106	286	819	64	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	5.68e-106	286	819	64	580	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5LM8_A	1.64e-94	283	802	17	525	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.69e-94	283	802	18	526	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	1.79e-94	283	802	45	553	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A067XMP2|PTAK_PESFW	5.14e-145	286	819	61	585	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|Q96WM9|LAC2_BOTFU	1.66e-109	284	805	63	568	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|J5JH35|OPS5_BEAB2	5.93e-109	284	819	68	590	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q0CCX6|GEDJ_ASPTN	1.99e-100	282	819	52	605	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|Q12570|LAC1_BOTFU	1.07e-95	283	819	60	561	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000334	0.999630	CS pos: 22-23. Pr: 0.9722

TMHMM  Annotations     

There is no transmembrane helices in KIW07853.1.