ID A0A091URC4_PHALP Unreviewed; 1314 AA.
AC A0A091URC4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Peroxidasin {ECO:0000313|EMBL:KFQ79678.1};
DE Flags: Fragment;
GN ORFNames=N335_05690 {ECO:0000313|EMBL:KFQ79678.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ79678.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ79678.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ79678.1};
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; KK461914; KFQ79678.1; -; Genomic_DNA.
DR PhylomeDB; A0A091URC4; -.
DR Proteomes; UP000053638; 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; cd09826; peroxidasin_like; 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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR034824; Peroxidasin_peroxidase.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF54; PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13855; LRR_8; 2.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 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; 3.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Reference proteome {ECO:0000313|Proteomes:UP000053638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 211..299
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 307..393
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 398..483
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 486..577
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT BINDING 1039
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:KFQ79678.1"
FT NON_TER 1314
FT /evidence="ECO:0000313|EMBL:KFQ79678.1"
SQ SEQUENCE 1314 AA; 147834 MW; 5DA84F1B882EF0A8 CRC64;
CPSRCLCFRT TVRCMHLMLE TIPDIPPQTN ILDLRFNHIK EIQPGAFRRL KNLNTLLLNN
NQIKQIVRRS FEDLENLKYL YLYKNEIQSI QQHAFNGLHS LEQLYLHFNN LESLEPETFS
DLPKLERLFL HNNKISRIHP GTFSQLESLK RLRLDSNALL CDCDLMWLAE LLKKYAEQGS
IQTAATCEAP RELHGRSIVT LTAQEFNCQR PRITSEPHDV DVLLGNTVYF TCRAEGNPKP
AIIWLHNNNK IDMKDDNRLN LLQDGTLMIQ NTKESDKGVY QCMAKNIAGE VKTQEVVLRY
FGTPSKPTFV IQPQNTEVLI GESVTLECGV SGHPHPRISW TLGTGSPLPQ DSRFAITSSG
GLFIQNVTFS DQGQYNCNAS NTEGSIQATA RIIVQDSPRF LLIPTDQTVT EGQSVDFPCS
AEGHPPPVIA WTRAGGPLPN DRRHSILSAG TLRVMRVALH DQGQYECHAI SAIGVRTLPV
QLSVTPRVIP VFLHPPQDVV AETGQDVAIT CIAQGDPRPT ITWVKEGIQI TESGKFHISQ
DGTLSIQDLG VADQGRYECI ARNPFGFTSS AMQLTITATD VGRSGDTFVA TSIREAISSV
DHAINSTRTE LFSKRPKTPN DLLALFRYPR DPYTLETARA GEIFERTLQL IQEHVQQGLI
VDMNVTGYRY NDLVSPHYLN MIANLSGCSA HRRTPNCSDI CFHKKYRTHD GSCNNLQHPM
WGASLTAFQR LLKPAYQNGF NLPRGFSLAE DARDLPLPLP RLVSTAMVGT ETITPDDQFT
HMLMQWGQFL DHDLDQTVAA ISMSRFSDGA PCSEVCSNDP PCFSVMVPAN DPRVRNGRCM
FFVRSSPVCG SGMTSLLMNS VYAREQINHL TSYIDASNVY GSTEQESREL RDLNSQNGLL
KQGQVVPSSG KHLLPFAVGP PTECMRDENE SPVPCFLAGD HRANEQLGLT AMHTLWFREH
NRIAMELSSL NPHWDGDLLY HEARKIVGAQ MQHITYAQWL PKVLGEAGMK MLGEYKGYNP
NINAGILNAF ATAAFRFGHT LINPILYRLN ETFQPIRQGH IPLHKAFFSP FRIMQEGGID
PLLRGLFGVP GKMRVPSELL NMELTEKLFS MAHSVSLDLA AINIQRGRDH GIPPYNDFRV
FCNLSSAQEF EDLRNEIKNL EIREKLRSLY GTTKNIDLFP ALMVEDLVPG TRVGPTLMCL
LTTQFRRLRD GDRFWYENPG VFTPAQLTQI RQTSLARVIC DNSDHIQQLQ RDVFRVASYP
QGMVGCEEIP VVDLRLWQDC CEDCRTRGQF RALSQRFRSK RSPGFSYPEE NPAK
//
