ID A0A0T2L1N9_9MICO Unreviewed; 496 AA.
AC A0A0T2L1N9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Copper oxidase {ECO:0000313|EMBL:KRA25851.1};
GN ORFNames=ASD65_01585 {ECO:0000313|EMBL:KRA25851.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA25851.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA25851.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA25851.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA25851.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA25851.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRA25851.1}.
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DR EMBL; LMGU01000001; KRA25851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T2L1N9; -.
DR STRING; 1736570.ASD65_01585; -.
DR OrthoDB; 345021at2; -.
DR Proteomes; UP000051216; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd04232; CuRO_1_CueO_FtsP; 1.
DR CDD; cd13867; CuRO_2_CueO_FtsP; 1.
DR CDD; cd13890; CuRO_3_CueO_FtsP; 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; IPR002355; Cu_oxidase_Cu_BS.
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.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051216}.
FT DOMAIN 73..179
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 223..299
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 354..475
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 496 AA; 53874 MW; 5E673191D6D8E769 CRC64;
MIAMLIALPI VLLVVVVGIL IAVFVPFGRP TPPATGAVEF TQPMPIPPLA ESRVEDGVRV
FTLEAQTGTT DFVPEGSTPT LGYNGSYLGP TLVAQRGETV RVDVGNSLDE STTVHWHGMH
LPAAMDGGPH NPIAPGDTWH PEWAIDQPAA TLWYHPHLHE RTRAQVDAGL AGMFLLRDDT
ESALALPCTY GVDDFPVIVQ DRSFGTDGAF SGGLGTQFDG ALGDTILVNG ATTPYLDVST
EKVRLRLLNG SSARMYDFAL ADGRDFDLIA TDGGLLSAPV PTDRVPLSPG ERAEIIVTLR
PGETVAMRSL APDPALNAGS AAFDVFELRA AASLARSAEL PTVLADVPAP DLSDIAQERN
FVMSGHNIND RQMEMNRVDF VATVDTSELW TVRNENPLPH SFHVHDTQFR VVSIDGQAPP
ARLAGWKDTI ALESQREYRL LVRFEDYADP TTPYMYHCHL LWHEDQGMMG QFLVVQPGQQ
PALNRIEGDD DDNHGH
//
