ID C5M9C3_CANTT Unreviewed; 618 AA.
AC C5M9C3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Iron transport multicopper oxidase FET3 {ECO:0000313|EMBL:EER34177.1};
GN ORFNames=CTRG_02995 {ECO:0000313|EMBL:EER34177.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34177.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER34177.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; GG692397; EER34177.1; -; Genomic_DNA.
DR RefSeq; XP_002548698.1; XM_002548652.1.
DR AlphaFoldDB; C5M9C3; -.
DR STRING; 294747.C5M9C3; -.
DR EnsemblFungi; CTRG_02995-t43_1; CTRG_02995-t43_1-p1; CTRG_02995.
DR GeneID; 8298480; -.
DR KEGG; ctp:CTRG_02995; -.
DR VEuPathDB; FungiDB:CTRG_02995; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_7_3_1; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000002037; 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:0006826; P:iron ion transport; IEA:UniProtKB-KW.
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};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron transport {ECO:0000256|ARBA:ARBA00022496};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..618
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002953317"
FT TRANSMEM 556..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..144
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 152..298
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 361..499
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 599..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 70379 MW; 68E2463B0C844619 CRC64;
MRSASLFLLI CSLISVISAE THTWWFQTGW VNANPDGVFE RPMIGFNDTW PLPTLRVKKG
DRVQLYLNNG FDDRNTSLHF HGMFQNGTNQ MDGPEMVTQC PIPPGETFLY NFTVGDQVGS
YWYHSHTSGQ YGDGMRGVFI IEDDDFPYDY DEEVVLTLAE HYHDFSDELT PKFLSRFNPT
GAEPIPSNML FNETRNNTWK VEPNKTYLVR IVNIGRFVSQ YIWMEDHDFT IVEVDGVYVE
QNTTDLLYIT VAQRYSVLIT TKNETDKNYA FMNRVDIDML DVIPGDLELN GTNYIVYNED
ADLPEPYLLD SIDDFFDDFW LKPLSKEKLL DDADYTITLE VQMDNLGNGV NYAFFNNITY
AHPKVPTLMS VLSSGDDASN ELVYGTNTNS FVLQGGEVID IVMNNLDTGK HPFHLHGHVF
QLIERHEGVD DDEDPVAYNS SDHAEWPEYP MLRDTIYINP QSYAVLRFKA DNPGVWFFHC
HIEWHLDQGL AIVLIEDPEG IQKQESQQIT DNHKEICEKV GVPWEGNAAG NTENYLDLKG
ENVQHKRLPT GFTAKGIVAL VFSCIAGVLG LVAISYYGMT DIKNVEQRVA RDLDVDLDDD
DVEQLSEEGS SGSNSKQH
//
