ID A0A084FV90_9PEZI Unreviewed; 685 AA. AC A0A084FV90; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 11-NOV-2015, entry version 7. DE SubName: Full=Laccase {ECO:0000313|EMBL:KEZ39002.1}; DE EC=1.10.3.2 {ECO:0000313|EMBL:KEZ39002.1}; DE EC=1.10.3.3 {ECO:0000313|EMBL:KEZ39002.1}; GN ORFNames=SAPIO_CDS10367 {ECO:0000313|EMBL:KEZ39002.1}; OS Scedosporium apiospermum. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae; OC Scedosporium. OX NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ39002.1, ECO:0000313|Proteomes:UP000028545}; RN [1] {ECO:0000313|EMBL:KEZ39002.1, ECO:0000313|Proteomes:UP000028545} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ39002.1, RC ECO:0000313|Proteomes:UP000028545}; RA Vandeputte P., Rechenmann M., Bouchara J.-P.; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000028545} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IHEM 14462 {ECO:0000313|Proteomes:UP000028545}; RG RefSeq; RL Submitted (SEP-2015) to UniProtKB. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KEZ39002.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JOWA01000165; KEZ39002.1; -; Genomic_DNA. DR EnsemblFungi; KEZ39002; KEZ39002; SAPIO_CDS10367. DR Proteomes; UP000028545; Unassembled WGS sequence. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC. DR GO; GO:0008447; F:L-ascorbate oxidase activity; IEA:UniProtKB-EC. DR Gene3D; 2.60.40.420; -; 3. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR011706; Cu-oxidase_2. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR002355; Cu_oxidase_Cu_BS. DR InterPro; IPR008972; Cupredoxin. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07731; Cu-oxidase_2; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR SUPFAM; SSF49503; SSF49503; 3. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2. DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028545}; KW Copper {ECO:0000256|SAAS:SAAS00290979}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|SAAS:SAAS00056202}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00290991, KW ECO:0000313|EMBL:KEZ39002.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000028545}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 124 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 685 AA; 76067 MW; C11DAAF89780B251 CRC64; MPPLPFPLLP RRAFQPTKFL PALSAQPTCT TRMNLKSGFG DDRRDDENDE AYPMLQLAAP LDGGTPDRYS LDSEDPLADV ETKEKELGDD RRGGKKRRYA WRVSLGLSCI ILLILAGILL SYFFRQQSRD PEPGSTSGIA ESIVNSAELE LDTGFIISRV PKTREYVFNV TRQLAAPDGI EKPMILVNGQ SPGPLIEANT GDILRITVNN QMPEESTTIH WHGIDQRNSN WMDGVHGVTQ CGIPPGETFT YEFNVTGQRG SFWYHSHVSV QYTNGLFGPL IIHDPDEKVP HYDDEKIIMF GDHFHEDAEK LSALYLGPEH PWSPMMAGME PPPDNILMNG VHVSNCSTPP SMDPSSLTPD ASSHCAAGSL YTTRIRSGDQ TRFRLISHST STPFWVTIDN HTLEIVEIDG TEVEPIATTR IFVNPGQKYS VLVSANQTAG NYLLRATAAT SCFHLPRAAS TGLASVNYEA VGILSYDDIN ADAGVIGSPW DLQSKSNSVF GDEPWGQECD DLPFDIAKPV RQATAYEVGE RNFHYFSFER HSINNRIQTV INQTAYKPLV DDATLWNVTE QYSSNLDANA GPRKGQNFQV VGWGNKDYGD GRTIWNLENP IRRDTITVPG YSHVVLRIRA DNPGVWAIHC HILWHAEDGM TLAIAQRLDE LEEQLNALDA SGAGHSLRRR FCSAN //