ID A0A2G5B190_COERN Unreviewed; 574 AA.
AC A0A2G5B190;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cupredoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=COEREDRAFT_50900 {ECO:0000313|EMBL:PIA12771.1};
OS Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA12771.1, ECO:0000313|Proteomes:UP000242474};
RN [1] {ECO:0000313|EMBL:PIA12771.1, ECO:0000313|Proteomes:UP000242474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA12771.1,
RC ECO:0000313|Proteomes:UP000242474};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KZ303571; PIA12771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5B190; -.
DR STRING; 763665.A0A2G5B190; -.
DR OrthoDB; 64567at2759; -.
DR Proteomes; UP000242474; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 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; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000242474};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..574
FT /note="Cupredoxin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013639952"
FT DOMAIN 30..144
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 155..274
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 366..512
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 544..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 64195 MW; F3BD7806FCAC3646 CRC64;
MLSCRLILLL QTVISAYICH AARVVLDWDI GYIQVNRDGY NNRRAIGVNG ELPIPPIYVD
HGDTLIINVH NSLSAPTSIH AHGIFHNGTG YYDGAAMVTQ CGIPPGESYS YTIEARQVGT
YWIHGHSRHQ NSDGLRVPLI IREKFHQPIV DYDDEVLLYL EDWYPTESSE KMKEITEPGN
GSVPPPTYPF GLINGYNGNN SEPIRFTPGK RYRIRIISMA TTEWFKVQFP GHQVEVIEAD
GVNCFPQLVD GFDMGPGQRY SAVVTALDTD TYNMPYNVTL YADFVPHING LNPRYYQGLI
EYKEGAPAKQ LPLTDDKQLN WANDIEMQPY DMQPALPVDR QIELTSVSIV TVDKRSLRML
NKYPYTEPPV PSLFTAMTTG ELALDRDVYG PQAEALILKH QEVIEVKVNN PSGLVHSFHL
HGHTFQIVEY GPVDRDIIEI PAGLNLTIAD APVAPVRQFH GAPMRRDTLV TPEFQYVKFR
IRADNPGVWL FHCHMDTHFA AGLAVTFIEA PDVLQQRQIL PQNLQQMCLR QGIKASGNAA
GNDGYDFTGL PPVPQVQKVS DTSSFGNATP PSTN
//
