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Database: UniProt
Entry: M7P1D6_9GAMM
LinkDB: M7P1D6_9GAMM
Original site: M7P1D6_9GAMM 
ID   M7P1D6_9GAMM            Unreviewed;       573 AA.
AC   M7P1D6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:EMR13286.1};
GN   ORFNames=MPL1_05919 {ECO:0000313|EMBL:EMR13286.1};
OS   Methylophaga lonarensis MPL.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR13286.1, ECO:0000313|Proteomes:UP000012019};
RN   [1] {ECO:0000313|EMBL:EMR13286.1, ECO:0000313|Proteomes:UP000012019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MPL {ECO:0000313|EMBL:EMR13286.1,
RC   ECO:0000313|Proteomes:UP000012019};
RX   PubMed=23661481;
RA   Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA   Murrell J.C., Shouche Y.S.;
RT   "Draft Genome Sequence of Methylophaga lonarensis MPLT, a Haloalkaliphilic
RT   (Non-Methane-Utilizing) Methylotroph.";
RL   Genome Announc. 1:E00202-13(2013).
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:EMR13286.1}.
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DR   EMBL; APHR01000028; EMR13286.1; -; Genomic_DNA.
DR   RefSeq; WP_009726187.1; NZ_APHR01000028.1.
DR   AlphaFoldDB; M7P1D6; -.
DR   STRING; 1286106.MPL1_05919; -.
DR   PATRIC; fig|1286106.3.peg.1188; -.
DR   eggNOG; COG2132; Bacteria.
DR   OrthoDB; 9757546at2; -.
DR   Proteomes; UP000012019; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd13874; CuRO_2_CopA; 1.
DR   CDD; cd13896; CuRO_3_CopA; 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; IPR006376; Cu-R_CopA.
DR   InterPro; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034282; CuRO_2_CopA.
DR   InterPro; IPR034279; CuRO_3_CopA.
DR   NCBIfam; TIGR01480; copper_res_A; 1.
DR   PANTHER; PTHR11709:SF394; 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; PS00079; MULTICOPPER_OXIDASE1; 1.
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:UP000012019};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..573
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004082856"
FT   DOMAIN          33..144
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          225..313
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          428..551
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          348..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  64217 MW;  4300F69C34A1186D CRC64;
     MTIIRFWLTT VLAASLSFSA FANQTEYTLV IDREAVNITG KTVDRITING TIPGPILEFT
     EGDEAVVHVI NKLDEPTSVH WHGLLLPPKM DGVPGMGGFS GIAPGETFTY RFPLRQNGTY
     WYHAHSGTQE QDGHYAGMII HPKDHSPVEA DRDYVVLISD FHEHSGRRIM QNLKKSPHYY
     NFSQRTVGDF FADVRQQGWS KVWRDARDWG QMRMSPTDLA DVSGYTFLIN GKTAEQNWTG
     VFKPGERIRL RFINASAMSI YDLRIKGLPM TVVQADGQYV EPVTVDELRF AVAETYDVIV
     QPQSHDAFTI VAESIDRTGF ALGTLAPEIG MRGPQPTHRP RALLTMADMG HGHGHDHDHS
     NPSHSAPSEH SGHEGHEGHE GHEGDSQHQS IGILESSNSG WAQAGTPEGH TALRYADLRS
     LTRQPDNRPP SREIVVTLDG SMERFIWTLD GKKFGDPDFK PIQLDYNERV RIIFQNNTMM
     AHPMHLHGMF MQLENGQHPD YLPSKHVVNV PPGQQMSVLL TADEPGEWMF HCHLLYHMAA
     GMMGVMAVAE ADPTGEHTGH HQHHHGGHHH DHH
//
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