ID   A0A099ZH80_TINGU        Unreviewed;      1012 AA.
AC   A0A099ZH80;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=ferroxidase {ECO:0000256|ARBA:ARBA00013107};
DE            EC=1.16.3.1 {ECO:0000256|ARBA:ARBA00013107};
DE   Flags: Fragment;
GN   ORFNames=N309_06581 {ECO:0000313|EMBL:KGL80170.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL80170.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL80170.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL80170.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC         Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001830};
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   EMBL; KL892819; KGL80170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099ZH80; -.
DR   STRING; 94827.A0A099ZH80; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR   CDD; cd04224; CuRO_3_ceruloplasmin; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR024715; Factor_5/8-like.
DR   PANTHER; PTHR46806:SF7; COAGULATION FACTOR VIII; 1.
DR   PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 2.
DR   Pfam; PF07732; Cu-oxidase_3; 3.
DR   PIRSF; PIRSF000354; Factors_V_VIII; 3.
DR   SUPFAM; SSF49503; Cupredoxins; 6.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000354-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053641}.
FT   DOMAIN          41..151
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          254..300
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   DOMAIN          394..502
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          758..854
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          897..1010
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   DISULFID        123..149
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        224..305
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        474..500
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        577..658
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL80170.1"
FT   NON_TER         1012
FT                   /evidence="ECO:0000313|EMBL:KGL80170.1"
SQ   SEQUENCE   1012 AA;  114383 MW;  631AB205DA42CD98 CRC64;
     ASVYATRGAN RIGRVYKKAI FRQFTDDTYT QEIPKAAWLG FLGPVLKAEE EDVFIIHLKN
     FASRPYSVHP HGVFYDKDSE GALYPDGTGG KSKEDDFVVP GGNYTYTWPV RKDYSPTLSD
     PNCLTWIYHS HIDTPRDIAS GLIGPLLVCK KDDTSIERTG AANAFALMFS IVDENFSWYL
     DQNINTFCLE PTTVDKEDEG FQTSNRMHAI NGYIYGNLPG LEMCANDPMS WHLFGMGSEI
     DIHAAYFYGH TFTNRGQRAD VVGLFPATFI TAEMTPGNAG RWLITCQVNE HLRGGMEALY
     DVQFCQKNFS RPTPLSHKRL YYIAAEEVLW NYGPDGYDKF TGQGLNATGS ESAIYFTQGT
     DRIGGQYWKV QYVEYTDATF RKRKRRSEEL KHLGILGPVI KAEVGDTVLV TFANKAKRSY
     SIMAHGVSYS KLSEGAPYLD GYPKPGSHVK PGETFTYRWR VPENGGPTES DPPCLTYLYY
     SATDAVKDTN SGLVGPLLVC RKNTLNPDGT QKGIDREFYL LFSIFDENDS WYLNKNIEAF
     TGDPSKVDKD NEDFKESNKM HAVNGYLFGN LPGLAMCKDD KVSWHLIGLG SHYDMHGVQF
     QGNTITLRGT TRDGLALFPH LSGTALMQPD RVGTFNVVCR TFDHFVGGMK HLYEVSSCRN
     STPAKQQYGG VRLYYIAAEE VEWDYASNKS SAPKIYNISS NEESYGHVFL SQTEDLIGSK
     YKKVVYREYT NGNFTQRKVR TEEEEHLEIM GKDSCFNLGP LLHAEVGETI LIVFKNKASR
     PYSITAHGIE EVGCEEQVET PITLPEEINT YRWNVPERSG PGKTDPNCIT WVYYSTANFV
     KDTYSGLIGP LVICRKGILN ENGLRKDIDR EFTLLFMVFD ENKSWYLKEN IETYLHKNPD
     DFNHTKNFVE GNCKHAINGK IYNSLLSLTM NEGDTTNWYL IGMGNEVDVH TVHFHAQTFI
     FKVDKDHRAD VYDLFPGTFQ TVELIAENPG TWLLHCHVAD HIHAGMETTY TI
//