ID A0A1X7EQJ7_9ACTN Unreviewed; 635 AA.
AC A0A1X7EQJ7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Spore coat protein A {ECO:0000313|EMBL:SMF38142.1};
GN ORFNames=SAMN02745830_03153 {ECO:0000313|EMBL:SMF38142.1};
OS Streptomyces sp. Amel2xC10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF38142.1, ECO:0000313|Proteomes:UP000192930};
RN [1] {ECO:0000313|EMBL:SMF38142.1, ECO:0000313|Proteomes:UP000192930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF38142.1,
RC ECO:0000313|Proteomes:UP000192930};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FWZW01000006; SMF38142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7EQJ7; -.
DR SMR; A0A1X7EQJ7; -.
DR OrthoDB; 345021at2; -.
DR Proteomes; UP000192930; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13844; CuRO_1_BOD_CotA_like; 1.
DR CDD; cd13869; CuRO_2_PHS; 1.
DR CDD; cd13892; CuRO_3_PHS; 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; IPR033138; Cu_oxidase_CS.
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; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 4: Predicted;
KW Capsid protein {ECO:0000313|EMBL:SMF38142.1};
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:UP000192930};
KW Virion {ECO:0000313|EMBL:SMF38142.1}.
FT DOMAIN 76..110
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 153..219
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 472..614
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 121..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 69308 MW; 2A6AE0B1AFC210FE CRC64;
MIEQSDDRID PTAGVLADEV LAKEREQAPA PGELTPFAAP LTVPPVLRPA SDEVTRETEI
ALRPTWVRLH PQLPPTLMWG YDGQVPGPTI EVRRGQRVRI AWTNRIPKGS EYPVTSVEVP
LGPPGTPAPS TEPGRGGVEP NKDVAALPAW SVTHLHGAQT GGGNDGWADN AVGFGDAQLS
EYPNDHQATQ WWYHDHAMNI TRWNVMAGLY GTYLVRDDEE DALGLPSGDR EIPLLIADRN
LDTDEDGRLN GRLLHKTVIV QQSNPETGKP VSIPFFGPYT TVNGRIWPYA DVDDGWYRLR
LVNASNARIY NLVLIDEDDR PVPGVVHQIG SDGGLLPRPV PVDFDAALPV LSAAPAERFD
LLVDFRALGG RRLRLVDKGP GAPAGTPDPL GGVRYPEVME FRVRETCEED SFALPEVLSG
SFRRMSHDIP HGHRLIVLTP PGTKGSGGHP EIWEMAEVED PAGVQVPAEG VIQVTGADGR
TKTYRRTART FNDGLGFTIG EGTHEQWTFL NLSPILHPMH IHLADFQVLG RDAYDASGFD
LALGGTRTPV RLDPDTPVPL APNELGHKDV FQVPGPQGLR VMGKFDGAYG RFMYHCHLLE
HEDMGMMRPF VVLPPEALKF DHGGAHGGHG EGHTG
//
