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Database: UniProt
Entry: F9DXX1_9BACL
LinkDB: F9DXX1_9BACL
Original site: F9DXX1_9BACL 
ID   F9DXX1_9BACL            Unreviewed;       502 AA.
AC   F9DXX1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:EGQ20109.1};
GN   ORFNames=HMPREF9372_3652 {ECO:0000313|EMBL:EGQ20109.1};
OS   Sporosarcina newyorkensis 2681.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1027292 {ECO:0000313|EMBL:EGQ20109.1, ECO:0000313|Proteomes:UP000005316};
RN   [1] {ECO:0000313|EMBL:EGQ20109.1, ECO:0000313|Proteomes:UP000005316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2681 {ECO:0000313|EMBL:EGQ20109.1,
RC   ECO:0000313|Proteomes:UP000005316};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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:EGQ20109.1}.
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DR   EMBL; AFPZ01000115; EGQ20109.1; -; Genomic_DNA.
DR   RefSeq; WP_009498343.1; NZ_GL982998.1.
DR   AlphaFoldDB; F9DXX1; -.
DR   STRING; 759851.SAMN04244570_3031; -.
DR   eggNOG; COG2132; Bacteria.
DR   HOGENOM; CLU_009100_2_4_9; -.
DR   OrthoDB; 9757546at2; -.
DR   Proteomes; UP000005316; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd04232; CuRO_1_CueO_FtsP; 1.
DR   CDD; cd13867; CuRO_2_CueO_FtsP; 1.
DR   CDD; cd13890; CuRO_3_CueO_FtsP; 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   PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR   PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..502
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039288513"
FT   DOMAIN          95..209
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          239..332
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          383..502
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   502 AA;  56318 MW;  469662AB9F43E74C CRC64;
     MRIKMKITAL AISILVISGC SNANSQPDEE MDHSMMNDEE MDHSMMDMGD DMMEGHMSHD
     EVVSLNDSTG DNELQIPSIL ERDNKEEVAY TVRAQKGKTE IFDGIETTTY GYNGTFLGPM
     LRLDKGDTVK IRTINELDEN TTFHWHGLEV AADADGGPHD VIKPGEEKII EFKVEQEAAT
     LWFHPHPEGK TAEQVYNGLA GLIYIEDENS KSLGLPNDYG KNDIPLIFQD KIFDDKKQLN
     FSAAMNDDGT IGDTLLINGT HNPKLTVNKE KVRLRLLNGS NARNYTFKLN TGDSFVQIAT
     DGGFLNEPVS LKEVTLTPSE RAEIVVDFSQ LNTENDLALI NEDGSVLLPF EVSDESGVIS
     GIPGEMNNFS LTEEEKNLPV TKKVELFGMM DMVEINGKKF DPERIDFTQK QGVTEVWEIY
     NKPDMMGGMI HPFHIHGTQF KIISRNGEAP PENERGWKDS ISIQPDETVK IAIQFKHKGV
     YMFHCHILEH EDNGMMGQVK VE
//
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