ID A0A177DQ56_ALTAL Unreviewed; 627 AA.
AC A0A177DQ56;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Bilirubin oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CC77DRAFT_933762 {ECO:0000313|EMBL:OAG21518.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG21518.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG21518.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG21518.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KV441476; OAG21518.1; -; Genomic_DNA.
DR RefSeq; XP_018386939.1; XM_018534337.1.
DR AlphaFoldDB; A0A177DQ56; -.
DR STRING; 5599.A0A177DQ56; -.
DR GeneID; 29119931; -.
DR KEGG; aalt:CC77DRAFT_933762; -.
DR VEuPathDB; FungiDB:CC77DRAFT_933762; -.
DR OMA; YQLDVMS; -.
DR OrthoDB; 315590at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13866; CuRO_2_BOD; 1.
DR CDD; cd13889; CuRO_3_BOD; 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; 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.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..627
FT /note="Bilirubin oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008059685"
FT DOMAIN 77..181
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 231..308
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 357..488
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 560..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 69717 MW; 080123E15C6AB895 CRC64;
MKNYFSIGVA ALLASQALAG DDAWISPVYK EIFQNELPIP KDKVKSYTYT NKTTGNQIDF
YEVDVTPFTQ QVYRGLKPAR LVGYDGVSPG PTFRMKKGRE AIVRFKNHGD KDLSVHLHGS
YSRAPFDGWA EDTTKPGQYK DYYYPNKQSA RTLWYHDHAI HHTAENAYFG QAGFYILHDP
AEDALGLPSG AYDVPLALAS KQYNSDGTLF DPKDETDSLW GDVIHVNGQP WPYMKVEPRK
YRFRMLNTAI SRAFKLTLED PTAKKVPFHV IGADTGLMTK PVQSDNLEIS MAERWEIVVD
FSTYSGKNVT MKNARDVQAD EDYNSTDKVM RFVVGTSVSD TAGNGALPGS LRTVPFPPKK
SGIDRSFKFG RTNGQWTVNG VTFADVNNRI LAKPQRGAVE VWELENSSGG WSHPVHIHLV
DFQILTRTGG KRSVLNYEKE ALKDVVLLGV NEKVTVIARY APYDGVYMFH CHNLIHEDHD
MMAAFNVTSL ADFGYPETTK FIDPMEEKYR SKDINDHDNE EEHIYEKCAE LEALEAYTGP
EKLEDALVDY WANGGKGPST LVTSTRSASS SSSQATASST AQATTTSPPS VARVTSSSAA
ITSAPKATSS STKKDDKKTS TSSTRRR
//
