ID W2LFY9_PHYPR Unreviewed; 962 AA.
AC W2LFY9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Plastocyanin-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=L917_06123 {ECO:0000313|EMBL:ETL96346.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL96346.1};
RN [1] {ECO:0000313|EMBL:ETL96346.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL96346.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KI678923; ETL96346.1; -; Genomic_DNA.
DR AlphaFoldDB; W2LFY9; -.
DR EnsemblProtists; ETL96346; ETL96346; L917_06123.
DR VEuPathDB; FungiDB:PPTG_02544; -.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13844; CuRO_1_BOD_CotA_like; 1.
DR CDD; cd14448; CuRO_2_BOD_CotA_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR003689; ZIP.
DR PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF02535; Zip; 1.
DR SUPFAM; SSF49503; Cupredoxins; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 624..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 720..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 877..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 902..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 937..959
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..261
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 488..602
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 770..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 103602 MW; 66435FF7ABB6A444 CRC64;
MFSRALWSVS VSTNTWGGES PRGLYDLIPQ FASHSTHPGP STKSASSSSS LSSMIPSARS
TMSSAIALAL GAVALLSSTD ALTDLKTDWE AYVSVLTIPE VIDMTDGGAI DMQIGRSTHN
WTEDGSLAGS IYGYALKNST PTSPGPTIKV ARGVPINITW YNELEAPHLL QESVQYTLTQ
HASACYPYCG VPVVTHVHGM ESPARFDGLP FLSIYKNQSQ EFVYLNNQSA STKTYHDHSN
GLTRLNTWAG LVGAYIISDP ELESSLNLNI ETDIPLILTD RLISNTGKIM YSDDNCNEGA
TLWIPESFGS VNLVNGVVMP YVEIPPAQVR FRLVNAANAR HYNLTMPFAD KCQVVATDSG
FVGEPKALTE DLVIFPFERV EFVCDFSGVE DGMTYDLEDK QTSDQATPYD NRVMQFRILT
SLKTDTMKVK EIPSSLTPYK SLKELYEAGG KERTLILGEM ETELLCPTMS ILLYRSQQVN
TSGITGHLHC TKGTVEKWNF QNPTDDPHPF HWHLINAQCG ETEETVNTNQ LKDVVVIPNA
GDRKPDTITQ VCYVACTPGD YLLEGNTRGA KEFNFDTTDP YVAHCHILEH EENAMMAWFN
IQDVDDGYAD DNGITPNTQI TNTVIATAMG MSVLGGLATT LSVLVISVNR LNFLASPLAL
SVAFALSSGV MLFIGLADLF EEAVTFYRAH YTTGNVDPEA YEKGGSASTG VCDNTCNGNA
YLTTVAAFFG GVVIILLVEF LVHSVFERKN AAGEKANAVD VGEMEEGDKA AFASPVPESP
AAANHELHSP STAESSNLLE QNAGQKEEYR RAGVMTGIAV AIHNFPEGLA LFVSSLAGLR
SGIVLSIGII LHNFPEGVAV AAPVYYATGS KLEAFKWTAL SGIAQPFGAA IGWAAVSGGM
SFALQASLYG IVAGMLVCIT VKELLPGAYK FDPSGKAFVV AFFSGLGIIA LSIMALKYAG
SS
//