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Database: UniProt
Entry: A0A091F7L0_CORBR
LinkDB: A0A091F7L0_CORBR
Original site: A0A091F7L0_CORBR 
ID   A0A091F7L0_CORBR        Unreviewed;      1413 AA.
AC   A0A091F7L0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Peroxidasin {ECO:0000313|EMBL:KFO65231.1};
DE   Flags: Fragment;
GN   ORFNames=N302_01845 {ECO:0000313|EMBL:KFO65231.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO65231.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO65231.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO65231.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KK719741; KFO65231.1; -; Genomic_DNA.
DR   STRING; 85066.A0A091F7L0; -.
DR   Proteomes; UP000052976; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd05745; Ig3_Peroxidasin; 1.
DR   CDD; cd05746; Ig4_Peroxidasin; 1.
DR   CDD; cd09826; peroxidasin_like; 1.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR047018; Peroxidasin_Ig-like3.
DR   InterPro; IPR034828; Peroxidasin_Ig-like4.
DR   InterPro; IPR034824; Peroxidasin_peroxidase.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   PANTHER; PTHR11475:SF75; PEROXIDASIN HOMOLOG; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07679; I-set; 4.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF00093; VWC; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00406; IGv; 4.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   PROSITE; PS51450; LRR; 2.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          179..265
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          275..361
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          366..453
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          454..543
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1346..1404
FT                   /note="VWFC"
FT                   /evidence="ECO:0000259|PROSITE:PS50184"
FT   COILED          1322..1349
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         1007
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO65231.1"
FT   NON_TER         1413
FT                   /evidence="ECO:0000313|EMBL:KFO65231.1"
SQ   SEQUENCE   1413 AA;  159484 MW;  DE0FC5C38CAD2B9F CRC64;
     DLRFNRIKEI QPGEFRRLKN LNTLLLNNNQ IKRIPSGAFE DLENLKYLYL YKNEIQSIDR
     QAFKGLASLE QLYLHFNQIE TLEPESFTHL PKLERLFLHN NRIAHLIPGT FSHLESMKRL
     RLDSNALHCD CEILWLAELL KTYAESGNAQ AAATCEYPRR IQGRSVATIT PEELNCERPR
     ITSEPQDVDV TSGNTVYFTC RAEGNPKPEI IWLRNNNELS MKEDSRLNLL DDGTLMIQNT
     QETDQGIYQC MAKNVAGEVK TQEVTLRYFE SPARPSFVIH PQNTEVLVGE SVTLECSATG
     HPQPRITWTK GDRTPLPNDP RVTITPSGGL YIQNVKQEDS GEYTCFATNS VDNIHATAYI
     IVQALPQFTV TPQDKTVIEG QTVDFPCEAK GYPQPVIAWT KGGGQLSVDR RHLVLSSGTL
     RISRVALHDQ GQYECQAVNI IGSQRIVVYL TVQPRVTPVF ASVPSDMTVE VGTNVQIPCS
     AQGEPEPVIT WNKDGVQVTE SGKFHVSPEG FLTIRDVGTA DEGRYECVAR NTIGYSSVSM
     VLSVNVPNVS RNGDPFVQTS IVEAIATVDR AINSTRTHLF DSRPRSPNDL LALFRYPRDP
     YTVEQARAGE IFERTLQLIQ DHVQDGLMVD LNGTSYHYND LVSPQYLNLI ANLSGCTAHR
     RVNNCSDMCF HQKYRTHDGT CNNLQHPMWG ASLTAFERLL KSVYENGFNL PRGIEPRRLS
     NGYALPMPRL VSTTLIGTET VTPDDQYTHM LMQWGQFLDH DLDLTVAALS EARFSDGQHC
     SSVCTNDPPC FSIMIPPNDP RVRNGARCMF FVRSSPVCGS GMTSLLMNSV YPREQINQLT
     SYIDASNVYG SSDHEALEIR DLASQRGLLR QGIVQRSGKP LLPFATGPPT ECMRDENESP
     IPCFLAGDQR SNEQLGLTSI HTLWFREHNR IATELLKLNP HWDGDTIYHE TRKIVGAEMQ
     HITFSHWLPK IFGEVGMKML GEYKGYDPSV NSGITNEFAT AAFRFGHTLI NPFLYRLDEN
     FEPIPQGHLP LHKAFFSPFR IVNEGGIDPL LRGFFGVAGK MRVPSQLLNT ELTERLFSMA
     RTVALDLAAM NIQRGRDHGI PPYHDFRVYC NLSSAQTFED LKNEIKNPDI REKLSRLYGS
     PLNIDLFPAL MVEDLVPGSR LGPTLMCLLS TQFRRIRDGD RLWYENPGVF TPAQLTQIKQ
     TSLARVLCDN GDNITRVQHD VFKVAEFPHG YSSCEDIPKL DLRMWQDCCE DCRTRGQFNA
     FSYHFRGRRS LDYSFREDKP LKKMKTAKTV SSVKQSKYFR NATSASNENR NVPAVNDFKE
     FVLEMQKTIS SLRNQIKKLE SRLSNSDCTD EEGKSYSSNE TWKRDPCTLC ECKVGQITCF
     VESCPPADCE APVKGKGDCC PVCLQQNTNK KKP
//
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