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
//