ID   A0A1M6BSG6_9FLAO        Unreviewed;       967 AA.
AC   A0A1M6BSG6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:SHI51725.1};
GN   ORFNames=SAMN05443429_102107 {ECO:0000313|EMBL:SHI51725.1};
OS   Cruoricaptor ignavus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Cruoricaptor.
OX   NCBI_TaxID=1118202 {ECO:0000313|EMBL:SHI51725.1, ECO:0000313|Proteomes:UP000184335};
RN   [1] {ECO:0000313|EMBL:SHI51725.1, ECO:0000313|Proteomes:UP000184335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25479 {ECO:0000313|EMBL:SHI51725.1,
RC   ECO:0000313|Proteomes:UP000184335};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQYI01000002; SHI51725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6BSG6; -.
DR   STRING; 1118202.SAMN05443429_102107; -.
DR   Proteomes; UP000184335; 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; 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; 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   InterPro; IPR045800; HMBD.
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   Pfam; PF19335; HMBD; 3.
DR   SUPFAM; SSF49503; Cupredoxins; 3.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   4: Predicted;
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:UP000184335};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..967
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012725753"
FT   DOMAIN          26..49
FT                   /note="Heavy metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF19335"
FT   DOMAIN          86..194
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          272..359
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          501..527
FT                   /note="Heavy metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF19335"
FT   DOMAIN          562..587
FT                   /note="Heavy metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF19335"
FT   DOMAIN          656..767
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          444..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   967 AA;  110121 MW;  7A7C76607E9FBAE3 CRC64;
     MKQLLTLLFS VIFSLAVFAQ DKAAFSCPMH PEIVAEAPGK CPKCGMNLVS GKAHHHHKAD
     DAKANDEKVS FGGKKVRYDL YARDTIVNFT GKKRRAIAVN GSLAAPTLHF TEGDTAEIYL
     HNQLKESASF HWHGVILPNP QDGVPFLTTK LIKPGDSHLY TFKVSQNGTY WYHSHSRLQE
     QIGMNGVLVF HKRNDSKKNY YKADIPVLLG EWSDEKPEEI MRRLHMNNTE WYAIKKKAVQ
     SYSEAIQKGH FFTKLKNEWK RMEAMDISDV YYEKFLINGK VADEYRNLSA GDKVRLRVVN
     GGSSSYFWLN FGGGKFKVIA NDGNDVEPVE VDRLIVGNSE TYDIEIEIPQ NKSYEFRATA
     EDRSGYASLW LGSGEKVEAP TLPRLELFEG MKMMNSMMKM SGDMKPMNMT MSNQTMDMNS
     VMYPELPKHE REMMMKHMDE MMDMSNVDGH SHHHSSHENH SEHSMHHHSQ HSENHEGKSC
     CSDKNHSHEN GHNCEHSEAE KFTCPMHPEI ISNEKGKCPK CKMDLVPMKN GGKNHEGKHC
     CSDKNHSHEN GHNCEHSDAE TFTCPMHPEI ISNEKGICPK CKMDLVPMKN AGKNLEGKSC
     CSDKNHSHEN GHDSHSHSAN HGEHSNHESS IVTLNYDMLA APEKNILPTE NVRTLKFTLE
     GNMLHYLWSL DNKTVLESDK ILIKKGEVLR IEMYNNSMMR HPMHLHGHDF RLLNAKGDYA
     PLKNVVDIMP METNTIEFPA NQDGDWFFHC HILYHMMGGM GRVFSYENSA ANPQLPNQKE
     AWRKFKNDNR MFSTMGMLGV QTNMLHADAM AMLGARYAAF ADVHYGYHHK DLEAEVKAGR
     YLGKFQWAMP YISYRFRNPM SYEMATEKKT MFGQQKVGKY RNTAAIGLEY VLPFLIMGDA
     SVDINGKFLL SLSREDIPLS PRFRGNFMVN TDREFSAGIS YILSRYISLS AGYDNHSGFG
     GGINFVY
//