ID A0A0D7B4S6_9AGAR Unreviewed; 632 AA.
AC A0A0D7B4S6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:KIY65195.1};
GN ORFNames=CYLTODRAFT_445510 {ECO:0000313|EMBL:KIY65195.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY65195.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY65195.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY65195.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KN880600; KIY65195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7B4S6; -.
DR STRING; 1314674.A0A0D7B4S6; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709:SF488; LACCASE-RELATED; 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; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..632
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002317063"
FT DOMAIN 40..153
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 180..375
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 496..616
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 632 AA; 69051 MW; C2A101711D5DD82D CRC64;
MVFLSPLSVF ASLFLGLVAT AKFVDVKTNE DGVAYHNITV SEGAYSPDGG RERLVYFIND
EFASHVVGVD EGAMLHIQIK SEISSPFTLH SHGIYQRESV WMDGVPGVTQ KPIMPEETFT
YKFKVDQSGM YHMHSHYKAL QDDGLYMGLL VRPSISKEKP FAQISPDDED LISKAEQNAY
AILLADYRRY TSSELQKVWD DTHIEPVCAN AILFNGQGSA VCPPRAEINA MSAGANLSSQ
GCRWPDDPFV NMFPDIGKPE AVPLEIYECD TSAVNSPLYS IEVNKTDGWA VFDFVNAGGL
WQLTVSVDEH PMWISAIDGE YVNVTEPVDS FAIQAGSRFQ AAIKLDGNPG DAFNIHAAAH
SSVQMITGYA ILQYASDASG VMAKLVSPAD GYPALANSTA YISYNGESLT TSDGLRANAT
TFDPSGPQAA PFIASVPPPS DEVTQTFIYC TIGRPNATHY AMNGTGMQPS MYEDSNPLIW
QSVYQRFLNG TTNDSIANAH SIEVIDKLNS TVDLIISVPF HNSPQHPIHK HLNKFWVIGM
GTGVWNWSSV AEAAKDTPES FNFVNPPVRD GFNTPETFDA DGAWLALRYV TDTAGPSALH
CHLSQHLGGG MLSVALQDMN DLKLPSEYDQ PR
//
