ID A0A239MDQ9_9ACTN Unreviewed; 467 AA.
AC A0A239MDQ9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Multicopper oxidase with three cupredoxin domains (Includes cell division protein FtsP and spore coat protein CotA) {ECO:0000313|EMBL:SNT39969.1};
GN ORFNames=SAMN05216276_103964 {ECO:0000313|EMBL:SNT39969.1};
OS Streptosporangium subroseum.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=106412 {ECO:0000313|EMBL:SNT39969.1, ECO:0000313|Proteomes:UP000198282};
RN [1] {ECO:0000313|EMBL:SNT39969.1, ECO:0000313|Proteomes:UP000198282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNT39969.1,
RC ECO:0000313|Proteomes:UP000198282};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FZOD01000039; SNT39969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239MDQ9; -.
DR Proteomes; UP000198282; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd13853; CuRO_1_Tth-MCO_like; 1.
DR CDD; cd13900; CuRO_3_Tth-MCO_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; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR PANTHER; PTHR11709:SF520; V-SNARE COILED-COIL HOMOLOGY DOMAIN-CONTAINING 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 Capsid protein {ECO:0000313|EMBL:SNT39969.1};
KW Cell cycle {ECO:0000313|EMBL:SNT39969.1};
KW Cell division {ECO:0000313|EMBL:SNT39969.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000198282};
KW Signal {ECO:0000256|SAM:SignalP}; Virion {ECO:0000313|EMBL:SNT39969.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..467
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012196016"
FT DOMAIN 63..173
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 210..287
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 356..464
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 21..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 51578 MW; F09CD9C9062CBE5A CRC64;
MMRSRIGPAC LAAALAITTV SGSDAGPSPP PPVREGAPLR DPPQLVSHNG ILRARLVVEG
RQVDVAGRKL WALTYNGHYM PPTLRIRPGD RLELAMENRL GKYTNLHVHG LHVSPSGHSD
NVFVHIHPGQ TFHYSYRFPA NLASGTYWYH SHAHPMSGPQ VAGGLSGIIV VDGLKRYLPP
DLRDITEHVI ALKDFQIQGN TVKTKDLHIS APTNRTVNGQ LNPTIRIRPG EIQLWRLSNI
SANIYYKVRL QGQPFQVIAH DANPVNRIWA ADSLLLAAGA RFDVLVRGGP PGRTQLQTLP
YNTGPAGNRF PQATLATLVS EGALTHPTAP PTTFAPTEDL SHAVLAARRT VVFSENKAGT
EYYINGRQFD PNRVDIRSKL NTVEEWTVRN DSNEEHSFHV HTNDFQLMSI NGRPHEGHGW
QDTVSIPPNG QIVIRMPFTD YTGRTVLHCH ILNHEDAGMM AVLEIVK
//
