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Database: UniProt
Entry: A0A1V8UST4_9PEZI
LinkDB: A0A1V8UST4_9PEZI
Original site: A0A1V8UST4_9PEZI 
ID   A0A1V8UST4_9PEZI        Unreviewed;       595 AA.
AC   A0A1V8UST4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Iron transport multicopper oxidase FET3 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B0A51_06945 {ECO:0000313|EMBL:OQO26383.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO26383.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQO26383.1}.
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DR   EMBL; NAEU01000215; OQO26383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8UST4; -.
DR   STRING; 1974281.A0A1V8UST4; -.
DR   Proteomes; UP000192386; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:InterPro.
DR   CDD; cd13851; CuRO_1_Fet3p; 1.
DR   CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR   CDD; cd13899; CuRO_3_Fet3p; 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   InterPro; IPR044130; CuRO_2_Fet3-like.
DR   PANTHER; PTHR11709:SF361; IRON TRANSPORT MULTICOPPER OXIDASE FET3; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..595
FT                   /note="Iron transport multicopper oxidase FET3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013116768"
FT   TRANSMEM        555..577
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..145
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          156..302
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          363..498
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   595 AA;  65198 MW;  50D326822687B027 CRC64;
     MALSLSNFLV CCAGFVAVAR SATHEYDWNI GWVRANPDGM AERPVMGING QWPLPTLNFT
     KGDRVIATVH NQLGNQSTSM HFHGLFQNGT NDMDGPVGVT QCGIPPGSSF TYNFTIDQPG
     TYWYHSHTRG QYPDGLRGQF LVHDPDGPYI GQYDEEIAIT LSDWYHDEMP GLLSHFISVA
     NPTGAEPVPD SALMSDTQNL SVAVQPGKTY LFRMTNMGAF AGQYFWIEGH SMRVVEVDGV
     HTEPAETDMI YLTAAQRYSF MVTMKDDVEG NFAMVGSMDT DLFDALPDGL DNNVTGWLVY
     DDAASKPAPV LIDAFEPFDD YTLVPQDGLE IYDHVDHSIQ LDMKMDNLGD GANYAFFNDI
     TYVEPIVPTL YSVLTTGDNA SNPTIYGVNT NSFVLEKGQV VEIVLNNDDA GKHPFHLHGH
     NFQVVWRSDE NDGFWNPDNT SAIESFPRKP MRRDVVMVNP QGNFVIRFKA DNPGVWLFHC
     HIDWHTASGL VATMIEAPLE LQSSMKIPAD HYQVCQDSGT PTAGNAAGNT ADVLDLTGQH
     KSPAPLPAGF TARGIVALVF SCLSAFIGMA VIAWYGAAPI AVRKTSVAAG KVTTN
//
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