CAZyme Information: XP_003437486.1

Basic Information

• Species: Podospora anserina
• Lineage: Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
• CAZyme ID: XP_003437486.1
• CAZy Family: GT48
• CAZyme Description: Podospora anserina S mat+ genomic DNA chromosome 6, supercontig 4 [Source:UniProtKB/TrEMBL;Acc:B2ANJ0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
568		62444.07	4.9566

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PanserinaSmat	10888	515849	370	10518

• Gene Location: location=CU633872:769040-770797(-)

Full Sequence      

MRFSFFFGTFLGWATWTVAVPLEHTKRQSCANGPTARNCWGDFSIDDDVTYTWPDTGVTR
SYSFDVGLATLAPDGVEKVMMVVNGQYPGPTIEANWGDSVQVEVCNNLSQNGTSIHFHGV
RHLNTNHADGAVSQTECPIAPGDCHTYRFKATQHGSSWYHSHYSLQYGDGLLGAIVIHGP
TTANWDIDLGPLLITDHYHESVFDLADEPLTSLIGIPPVAVNGLMNGKNAYLTGTGSRAE
FTFTPGKKHLLRLVNTGSEMIFRFAVDQHRMTVVAMDFIPIQPFETDTLLIAIGQRYDVI
IEADQSPDVAYWARGVPMTSCFAINLMSTDIRAIVRYESDTPVTGDPTSTSWLMLDTCAD
EDLSNLVPHITHSVGPSALTQNFNAVLLPSQGDNYAVRWRVGGSEPYRPPKNNPVVKQVI
DTAAVNLTADFNPIDLTSLAPSSWVYLIVESLAPLPHPLHLHGHDTYVLARGTGPYVELL
TSLDLESPPRRDTFNLPQSGYVVLAFQTDNPGSWLLHCHIQWHIHQGFALTLVEGSPSSI
QGVYGSGEDAEMRRVCQNWVSSGLETTD

Enzyme Prediction     

EC	1.10.3.2:4	1.10.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	48	358	1.1e-125	0.9903846153846154

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259923	CuRO_1_MaLCC_like	1.47e-72	57	178	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.
274555	ascorbase	2.00e-70	59	542	1	537	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	2.18e-67	56	535	20	547	L-ascorbate oxidase
215324	PLN02604	3.56e-63	59	542	24	560	oxidoreductase
259947	CuRO_2_MaLCC_like	1.98e-61	189	352	1	163	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAP65571.1|AA1_3	0.0	1	568	1	568
CDP31566.1|AA1_3	0.0	1	568	1	568
VBB84816.1|AA1_3	0.0	1	568	1	568
ACR16059.1|AA1_3	7.87e-196	17	559	18	551
QQX29064.1|AA1_3	4.61e-150	32	559	61	584

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3V9E_A	1.18e-141	21	559	31	564	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.18e-141	21	559	31	564	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]
5LWX_A	7.68e-130	19	534	13	532	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
5LM8_A	1.30e-129	40	534	4	504	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	1.34e-129	40	534	5	505	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|J5JH35|OPS5_BEAB2	1.14e-146	17	559	31	573	Oxidoreductase OpS5 OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=OpS5 PE=1 SV=1
sp|Q96WM9|LAC2_BOTFU	2.19e-144	29	559	38	565	Laccase-2 OS=Botryotinia fuckeliana OX=40559 GN=lcc2 PE=2 SV=1
sp|Q12570|LAC1_BOTFU	2.71e-137	20	559	27	545	Laccase-1 OS=Botryotinia fuckeliana OX=40559 GN=lcc1 PE=2 SV=3
sp|Q0CCX6|GEDJ_ASPTN	1.53e-120	16	559	7	585	Dihydrogeodin oxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=gedJ PE=1 SV=1
sp|A0A067XMP0|PTAE_PESFW	1.98e-112	29	559	25	590	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
0.000657	0.999326	CS pos: 27-28. Pr: 0.5583

TMHMM  Annotations     

There is no transmembrane helices in XP_003437486.1.