ID A0A091R4N7_MERNU Unreviewed; 1237 AA.
AC A0A091R4N7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peroxidasin {ECO:0000313|EMBL:KFQ33841.1};
DE Flags: Fragment;
GN ORFNames=N331_12584 {ECO:0000313|EMBL:KFQ33841.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ33841.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ33841.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ33841.1};
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; KK711805; KFQ33841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091R4N7; -.
DR Proteomes; UP000052967; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
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 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; 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; 3.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF00093; VWC; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00406; IGv; 3.
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 PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 3..89
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 99..185
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 190..277
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 278..367
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1170..1228
FT /note="VWFC"
FT /evidence="ECO:0000259|PROSITE:PS50184"
FT COILED 1146..1173
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 831
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:KFQ33841.1"
FT NON_TER 1237
FT /evidence="ECO:0000313|EMBL:KFQ33841.1"
SQ SEQUENCE 1237 AA; 139090 MW; F4031AB3E7FAE06F CRC64;
ERPRITSEPQ DVDVTSGNTV YFTCRAEGNP KPEIIWLRNN NELSMKEDSR LNLLDDGTLM
IQNTKETDQG IYQCMAKNVA GEVKTQEVTL RYFESPARPS FVIHPQNTEV LVGESVTLEC
SATGHPQPRI TWTKGDRTPL PSDPRITITP SGGLYIQNVK QEDSGEYTCF ATNSIDNIHA
TAYIIVQALP QFTVTPQDKT VIEGQTVDFP CEAQGYPQPV IAWTKGGGQL SVDRRHLVLS
SGTLRISRVA LHDQGQYECQ AVNIIGSQRI VVYLTVQPRV TPVFASVPSD MTVEVGTNVQ
IPCSAQGEPE PVITWNKDGV QVTESGKFHV SPEGFLTIRD VGTADEGRYE CVARNTIGYS
SVSMVLSVNV PNVSRNGDPF VQTSIVEAIA TVDRAINSTR THLFDSRPRS PNDLLALFRY
PRDPYTVEQA RAGEIFERTL QLIQDHVQDG LMVDLNGTSY HYNDLVSPQY LNLIANLSGC
TAHRRVNNCS DMCFHQKYRT HDGTCNNLQH PMWGASLTAF ERLLKSVYEN GFNLPRGIEP
KRLSNGYALP MPRLVSTTLI GTETITPDDQ YTHMLMQWGQ FLDHDLDLTV AALSEARFSD
GQHCSSVCTN DPPCFSIMIP PNDPRVRNGA RCMFFVRSSP VCGSGMTSLL MNSVYPREQI
NQLTSYIDAS NVYGSSDHEA LEIRDLASQR GLLRQGIVQR SGKPLLPFAT GPPTECMRDE
NESPIPCFLA GDQRSNEQLG LTSIHTLWFR EHNRIATELL KLNPHWDGDT IYHETRKIVG
AEMQHITFSH WLPKIFGEVG MKMLGEYKGY DPSVNSGITN EFATAAFRFG HTLINPFLYR
LDENFEPIPQ GHLPLHKAFF SPFRIVNEGG IDPLLRGLFG VAGKMRVPSQ LLNTELTERL
FSMARTVALD LAAMNIQRGR DHGIPPYHDF RVYCNLSSAQ TFEDLKNEIK NPEIREKLSR
LYGSPLNVDL FPALMVEDLV PGSRLGPTLM CLLSTQFRRI RDGDRLWYEN PGVFTPAQLT
QIKQTSLARV LCDNGDNITR VQHDVFKVAE FPHGYSSCED IPKLDLRMWQ DCCEDCRTRG
QFNAFSYHFR GRRSLDYSFQ EDRPMKKIKM SKTVSSVKQS KYFRNATSAS NENRNMPAVN
DFKEFVLEMQ KTISSLRNQI KKLESRLSKT DCTDEKGKSY SSNETWKRDP CTVCECKVGQ
ITCFVESCPP ADCEAPVKVK GDCCPVCLKQ NINKKKP
//
