ID   A0A151JSE3_9HYME        Unreviewed;      1237 AA.
AC   A0A151JSE3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Peroxidasin {ECO:0000313|EMBL:KYN30130.1};
GN   ORFNames=ALC57_00413 {ECO:0000313|EMBL:KYN30130.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN30130.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN30130.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN30130.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN30130.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ978565; KYN30130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151JSE3; -.
DR   STRING; 471704.A0A151JSE3; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
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   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11475:SF109; CHORION PEROXIDASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492}.
FT   REGION          130..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         201
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"
SQ   SEQUENCE   1237 AA;  140549 MW;  585B01F72708B9C3 CRC64;
     MTVPTFVDLQ GIFVGKKFIV KEVAVLRKGA ILSHYIFTCP MPWSFLTKSE KYCSSWLSAY
     HHGLQVSSLL PEDAKLTLTQ IAEVIQLLAE GKSTADLAPI DEWLFGASFV DEVKDAQACE
     KVARLARAPA TTSKDSPHSA EEVQIAQRQA SQGNAKAPAR PQVMKIFDLE VHKKDYYKGY
     DPTVNPTIAN SFSTAAYRFG HSLVQRSFIR FDSDHRPIFN NVSIHDEFTN PVNLDTAGSV
     DRLLLGLVNQ PCQRRDEFIT EEMTNHLFQT PGFPFGMDLA SLNIQRGRDH GIPPYIRWRK
     PCSLSPIRTF EDLSKVMSLD IIRKLKSLYS SVDDIDLFSA GLAEKSVIGG LVGPTFACII
     AQQFSNLRRG DRFWYENPNS ESSFTAGQLQ QIRQVTLAQV LCQTMDDIKT IQPFVFLATD
     VLKNQRLSCD DLAIGHLSLE LWTEQPSEFK SNVDNSQKVK RAATDTSFSI SKLKEENIHP
     RRKIHPESNP EHTKVTTLKP FQNSINQENK IIVKRPLVHP NNNNVTIVVQ NNAVNALVFV
     NEGIYGSHIK IQEQLPINST FRPQEKPIPT TISHSSNFYL ARQPYVPYTF NDPHNPNPLV
     YGYRLPPFTQ DDISYDNYPA TSPRPTLYTY YTNFQQTITQ MPEIDGYLIN YGLSYHNLIP
     AYSYEKPKLL ENFGHNKLKE EQNPAKKKPN YADLKLLTNM EQNYCGYKPS TITQPNYVLN
     SEPYHTDKPS NDEHRSLTST QPNLQSNFGW NDKLYHGSDY NVVKLPCNSR PNEDLHHVQN
     LIYNGFTSLT NFRSDKSNQE SYGKQKLNGV RNLYLQNSDL INRLNEGHFI NLNKPQYQEQ
     WNLNDQKRLS KTPYDYDDLN LYQIKPNVKP PSYSVDMSHQ ILFTTKPSNE YNFQFWKKDS
     LQSIKNFVQS GLYGSVPSSE TNIPSYQKDT FTDSNISFPI NNNYNRYSGT TQIYQKILSS
     TQSGWLDVLS HIKQGNTQSL FSKNKYPYSS FLFNQTSTSY STYQKDDQSK ASLKVSGNKS
     FVDVDSHEHN SHKNPLKSSS LNEQLLSSTS YWLEISTTGI QVHKQEENSN PKRTKVQSVT
     IVNKTIEAVH HPGHTGYVSQ LKATSKISTP LVQQIKSNVS VTKKAGQYYY DKNVLYQYPD
     KIVNQSPKNN PYLTDKFDGT LIRNGKITSE KIAIETSVDK PITSSEMVQN ENKLTTTPTL
     LITAHGNHTG DVEDIQSDFS IDIGSVAPAD VPDRYFS
//