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Database: UniProt
Entry: A0A060JEE2_9MICO
LinkDB: A0A060JEE2_9MICO
Original site: A0A060JEE2_9MICO 
ID   A0A060JEE2_9MICO        Unreviewed;       487 AA.
AC   A0A060JEE2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:AIC47125.1};
GN   ORFNames=Rhola_00003020 {ECO:0000313|EMBL:AIC47125.1};
OS   Rhodoluna lacicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Rhodoluna.
OX   NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC47125.1, ECO:0000313|Proteomes:UP000067708};
RN   [1] {ECO:0000313|EMBL:AIC47125.1, ECO:0000313|Proteomes:UP000067708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC47125.1,
RC   ECO:0000313|Proteomes:UP000067708};
RX   PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA   Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT   "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater bacterium
RT   with stream-lined genome.";
RL   Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
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DR   EMBL; CP007490; AIC47125.1; -; Genomic_DNA.
DR   RefSeq; WP_038501913.1; NZ_CP007490.1.
DR   AlphaFoldDB; A0A060JEE2; -.
DR   STRING; 529884.Rhola_00003020; -.
DR   KEGG; rla:Rhola_00003020; -.
DR   PATRIC; fig|529884.3.peg.289; -.
DR   eggNOG; COG2132; Bacteria.
DR   HOGENOM; CLU_009100_2_1_11; -.
DR   OrthoDB; 345021at2; -.
DR   Proteomes; UP000067708; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11709:SF218; FI03373P-RELATED; 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; PS00080; MULTICOPPER_OXIDASE2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067708};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          68..180
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          237..302
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          367..484
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   487 AA;  53270 MW;  05FCADBF4CA44083 CRC64;
     MSNKTKKQLS RRNFLAIGGA VAGTAAIAGV SYSLLNPTNQ AQSGSEPERL VSKNGALGIS
     LVAAMTSKVI NGKTAKVMTY NGTSPGPTWV AKPGDVITVD FTNNLGDSTN LHTHGLHVSP
     EGNSDNTFIE VKDGETFTYK YQIPENHKEG TFWYHPHHHG MVAPQVFAGL YGGIIIENDE
     TPKVEEDRVV IISDISIASD GNVAGANMMS KMMGREGEVL LVNGQVQPVM EPKMWSVERW
     RIINSCTSRN LDLALTGAKA MVLGIDGNKY SQPRDLKRVT IAPGNRVDLL VTVTDKEASL
     TYTTVPHPDA MGMMGSATEY KDYPLVKFQP SKAAASIASL APMSFVQPDL RSLPVSAKRT
     FKLWMPSMNN MMDMMSTGLE GQFIINGKPF DGTRIDTSSA ANSVEEWTLV NESTMDHPFH
     LHVWDQQLVS VPNRLIQEVE YQDVVNVPAK SKVVVRVQFS DFAGMTVYHC HILDHEDLGM
     MGIINVI
//
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