ID Q50H78_9PEZI Unreviewed; 594 AA. AC Q50H78; DT 07-JUN-2005, integrated into UniProtKB/TrEMBL. DT 07-JUN-2005, sequence version 1. DT 22-NOV-2017, entry version 52. DE SubName: Full=Laccase I {ECO:0000313|EMBL:AAY33970.1}; OS Hortaea acidophila. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Dothideomycetes; Dothideomycetidae; Dothideales; Hortaea. OX NCBI_TaxID=245834 {ECO:0000313|EMBL:AAY33970.1}; RN [1] {ECO:0000313|EMBL:AAY33970.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15796994; DOI=10.1016/j.femsle.2005.03.007; RA Tetsch L., Bend J., Janssen M., Holker U.; RT "Evidence for functional laccases in the acidophilic ascomycete RT Hortaea acidophila and isolation of laccase-specific gene fragments."; RL FEMS Microbiol. Lett. 245:161-168(2005). RN [2] {ECO:0000313|EMBL:AAY33970.1} RP NUCLEOTIDE SEQUENCE. RA Tetsch L., Janssen M., Hoelker U.; RT "In search of the laccase genes of Hortaea acidophila."; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC {ECO:0000256|SAAS:SAAS00534212}. 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; AY351908; AAY33970.1; -; Genomic_DNA. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. 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; IPR033138; Cu_oxidase_CS. 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; 1. DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|SAAS:SAAS00524507}; KW Metal-binding {ECO:0000256|SAAS:SAAS00524516}; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00644416}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 594 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004248245. FT DOMAIN 95 209 Plastocyanin-like. {ECO:0000259|Pfam: FT PF07732}. FT DOMAIN 224 337 Plastocyanin-like. {ECO:0000259|Pfam: FT PF00394}. FT DOMAIN 438 567 Plastocyanin-like. {ECO:0000259|Pfam: FT PF07731}. SQ SEQUENCE 594 AA; 64494 MW; 2655A79B9C447C9B CRC64; MAAHLLLGAL MLGSALAISY HKPAWIPLGD SLSPRLGQDV TNGNGVLGTL DAPRLAKFLP DTHASRHRRK GYSPTDIGIG DVPVTGVTRY YNFTITEQNI APDGVVRSGM VVNGGYPGPT IEANWGDYFE ISVVNALPNE GTSIHWHGLI QHETPYMDGV PGIVQCPIAP GGNFTYRFRA DLYGTSFYHS HYSAQYTGGI YGAMIIHGPT ENAQYDEDIG PVLLNDWYHL PPPQSNNNLI NGKMNVSRQR CTPNAGISKF TFQSGKTYRL RLINAGAEGM QKFSIDGHTM TVIANDFVPL KPYQTDVVTL GIGQRSDIIV TATGKAGQSY WMRSDLGLNA LSNPAGCTNN DGVSPLALAA IYYEGADTNS VPTTNSTVPE SSIQSCMNDP LNMTVPYYSL TPSTTPAMSQ NIDITFASNG TNYLFYMNNS TFRADYNDPI LLEAKLGQTV FPAEENVIST GNASSVRFVL YNYAFTGAHP MHMHGHNYWV LAEGYGTWDG TVTNAGNPQR RDVQLLPPAQ VNADLVVTSP SYIVLQFNAD NPGVWPLHCH IAWHVSAGLY VSILENPTAI KSMHIPKPAA WTGKDVPDQI DSGL //