ID A0A074VI76_9PEZI Unreviewed; 322 AA.
AC A0A074VI76;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Di-copper centre-containing protein {ECO:0000313|EMBL:KEQ60213.1};
GN ORFNames=M437DRAFT_87047 {ECO:0000313|EMBL:KEQ60213.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ60213.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ60213.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ60213.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
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DR EMBL; KL584844; KEQ60213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VI76; -.
DR STRING; 1043003.A0A074VI76; -.
DR HOGENOM; CLU_865946_0_0_1; -.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 2.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF124; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..201
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|Pfam:PF00264"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 36288 MW; A8B99A1EDFCC308F CRC64;
MSQQTILSEK QQLAQELEKK QPQNNDLESQ SPGSPPPARP VFLLLWLLFV LGTVATIVSS
NWSKPDCLNK AQHILHKSTN PVTTSTSLPK SAPTSTCDNL TLRREWRSMK PLEQARYRSA
VRCLLDLPSK NDNTGNRLGD FLSAYSVSGW HATQTSDYLP WNRFFMHSLE SALRNECAYR
GDMPYLDWTV AAAYPESLGE PASATTASPQ AAFHDKLTKQ HLDPALVSEI MSAGTYDDFA
HVLEARITSL APFDLSSPEL PQDPLFLHQL QVDRLWWLWQ QQHPKAEMLV EDERVRLHGF
GNSIAVKSVA STEGYDLCYR YV
//