ID A0A2T3Z231_9HYPO Unreviewed; 579 AA.
AC A0A2T3Z231;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:PTB38800.1};
GN ORFNames=M441DRAFT_146142 {ECO:0000313|EMBL:PTB38800.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB38800.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB38800.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB38800.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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; KZ679265; PTB38800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3Z231; -.
DR SMR; A0A2T3Z231; -.
DR STRING; 1042311.A0A2T3Z231; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000240493; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd04205; CuRO_2_LCC_like; 1.
DR CDD; cd13910; CuRO_3_MCO_like_4; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709:SF515; ADR239WP; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493}.
FT DOMAIN 58..174
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 187..320
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 453..558
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 579 AA; 64017 MW; 0160CB410524C1A6 CRC64;
MRIVGLLIAL SLASVVVLIF AIDRHTRNLI DESQLAIPLH PVEHSTRDPT TLTFEWHVTQ
GTRTPDGVEK QVYLVNGHFP GPTIEGRSGD RIIVRVYNDL KDEGVSLHWH GLRMQGFNAM
DGAVGFTQCP ISPGTSFVYD FRIRDDEHGT FWWHSHNQLQ RADGLFGGLV IHEPRRRDAN
AALQDEALLL VGDWFHRKQS DVLAWYSSPA SAGKEPVPDS VVINGRGRYD CSMAVPARPV
KCEATALSDF PPLIKKSTGE TRLRVVNTGT VAGLTVGVDG ASLQPLEIDG GCKVDPKAAD
SVGTLYPGER VDLLLKWKSD RAAEPWFNVY LDHENLGFGN PALNPNHTFP ALPKTVTGHD
REHASLLKFR DHHVDLATLS STEEQTHIVT AEEEQTILFY ASTQTLAVNG NIPLGFMNHT
SWHPQSLPLL SQNRSSWDDK QLIPFIPSGS KPTKVKLVIN NLDDGSHPFH LHGYSFYVLS
SFRAESGSLG SYNPYATPES DSPGKWNRER PLRKDTVSVP RKGHVILSFV ADNPGMWMLH
CHMLVHMGTG MATGFQVGVP GDEEHIYGLD ESAARLCKA
//
