ID F2F8R5_SOLSS Unreviewed; 539 AA.
AC F2F8R5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:BAK15006.1};
GN OrderedLocusNames=SSIL_0583 {ECO:0000313|EMBL:BAK15006.1};
OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK15006.1, ECO:0000313|Proteomes:UP000006691};
RN [1] {ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA Morohoshi T., Someya N., Ikeda T.;
RT "Genome sequence of Solibacillus silvestris StLB046.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAK15006.1, ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK15006.1,
RC ECO:0000313|Proteomes:UP000006691};
RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT "Complete genome sequence and characterization of the N-acylhomoserine
RT lactone-degrading gene of the potato leaf-associated Solibacillus
RT silvestris.";
RL J. Biosci. Bioeng. 113:20-25(2012).
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; AP012157; BAK15006.1; -; Genomic_DNA.
DR RefSeq; WP_014822669.1; NC_018065.1.
DR AlphaFoldDB; F2F8R5; -.
DR STRING; 1002809.SSIL_0583; -.
DR KEGG; siv:SSIL_0583; -.
DR PATRIC; fig|1002809.3.peg.589; -.
DR eggNOG; COG2132; Bacteria.
DR HOGENOM; CLU_009100_4_0_9; -.
DR Proteomes; UP000006691; Chromosome.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13844; CuRO_1_BOD_CotA_like; 1.
DR CDD; cd13868; CuRO_2_CotA_like; 1.
DR CDD; cd13891; CuRO_3_CotA_like; 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; IPR008972; Cupredoxin.
DR PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006691}.
FT DOMAIN 106..188
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 250..336
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 408..525
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 539 AA; 62277 MW; D9A1F0520A2921E8 CRC64;
MKINDQPVNP ADPATISKFE DKLVIPRVAR SKPNNNYPPN SYYEIQMLKA RHRFHKDFPY
TDVWGYDGIV PGPTIEAKKD VTTYVKYLNK LPDKHFLPVD YSLHGVNNSA EVRTVVHLHG
ANVASASDGH PEAWYTKNYA ATGPLFKQEV HAYTNHQPGT TMWYHDHAMA LTRLNVVAGL
AGFYLLRDSL EERLKLPKGD YEIPLLIQDR SFNEDGSIFY PTKLDPPFPL PVPDQLPLPD
PTVTLGYVGN TVIVNGKVWP YLNVEPRKYR FRILNGSNRR SYKLRLSNEE EMNQIGTDGG
FLAATTKIIT AELNPAERID VIIDFSKFAN EEIFLMNDDE EFADEHTNVI MKFIVNLPLR
REDTSQIPTL LEPAMDLHEH HAHTIRNLPL TSSLDRYGRL MLMLDNKMYH DPATEKPSLD
SIEIWNFINT TPVHHPIHLH LVQFKILERR PFNVDLYVSE GKLEFTGEPE KPRDYERGWK
DTVKADIGKV TKIIMHWKEH TGDYMWHCHF LEHEDHDMMR PIRVINDAHP VQPPHIDDH
//
