ID A0A195FU35_9HYME Unreviewed; 1578 AA.
AC A0A195FU35;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE SubName: Full=Chorion peroxidase {ECO:0000313|EMBL:KYN43399.1};
GN ORFNames=ALC56_02125 {ECO:0000313|EMBL:KYN43399.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN43399.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN43399.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN43399.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN43399.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ981280; KYN43399.1; -; Genomic_DNA.
DR STRING; 34720.A0A195FU35; -.
DR Proteomes; UP000078541; 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:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09823; peroxinectin_like; 1.
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:SF106; CURLY SU; 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 Oxidoreductase {ECO:0000313|EMBL:KYN43399.1};
KW Peroxidase {ECO:0000313|EMBL:KYN43399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078541}.
FT REGION 885..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..933
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472
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 1578 AA; 181044 MW; E9A4D0AA564635AA CRC64;
MRIYDKRIKG GRQERNVDVE KRRRELLGQP SSAQPKSGTF QCHPTTAGGT QTCITFDAVN
HAYVEARKRI NVARPKSEMW RPEDLATVGE LLLDVTTNLA QTYGLTYEEI QRSLPLIDTS
KTLIREVCPA FLSNIECRPG KYRRFDGLCT NLENPTWGAT LSPFTRLMSP QFADGLSAPR
ISITGRDLPL SRVVSRTMHP DEGYHDHAGT VMVIAWGQFM DHDYTLTATP LDPLNRNDPE
ECCSRRPHQK NPYCNEILIP EDDYFYKLFN VQCMDFVRAF PAVRPGCRLG SRVPFNLLTG
VLDGNTVYGI TEAFARKLRT GYGGLLRMNP VFAEYGLKDL LPLKLDIPDE GCTRPNRSMY
CFEAGEIRVN EQLVLTCMHT LMAREHNRIA KALAVINPHW DDEILFQEAR RIVIAEIQHV
TYNEFLPILL GKDVMEKFGL LLEKEKYWDG YDSSINPGVI DAFAAAAFRF GHSLLPTAVE
RWSKAHKFIA SKRLSDLIRR PYDLYRAGVF DEYLMGLMNQ VAQAMDDSIT QEVTNHLFKK
VGAKFGLDLV SFNMQRGREF GIPSYMEFRK YCGLPDANTF DELFGSMPNE TVRRYSTIFD
GPIDAKNSVF GNNGFISAML LFRHPADVDL WSGGVSERPL PGSMLGPTFA CLIATQFSHS
RRGDRFWYEL PNQPSSFTLE QLNEIRKAKL ARLICDNTDL IDTVQIYPMV LPDHEINPRV
PCRSGIIPGI DLSKWAEFPA TSHAAEQYDT IMKSTQAAPE IKPTLQHAYI NKFNRKLKSM
GKNTAISSEK KSSKPWWIYP SVGWKKYTQR LKMPQKLLQQ QEEFLNKQIM SPTFHLMNNQ
NKNVDLSDPD MEIIKITTVV EAIRQKRQNS AQILKAAKSI QKIIGNKRSK RSSYKSGNNS
QDVQREKTII SNKKSRHPNP NRKQPKRTLS TKKPLRNKNA TDLKTANNVA IPSTLFYKRI
WEYINGTRPH TDIISGYNSL ENNSDNSTCT DKDRITGSQS QEDKSQVTST NIKPERDFYK
RIWDLINATQ SIRNEKTRSK RNASIPESSA ASTPCIQEET VNYKEDKQGV QATNDKTLNI
TDINLPEISD SGPYISGFWN IANKIQWQPN QIPVVEAKLN NNPILSSLIT SASEVDDLNK
FSDKVESVDY SSLDNSTEYT NEMRNSSQEI ISEPGSPYSS EESFTTSSFL PTESAVEKPL
QEKNQVERRE NLTGTIPNYD PSNIPYVEVP DYSDQQEKSL DKNNQSITPV RYNEYDDSDY
DYIPKQLHDA DDFSSKSPSA KIKVVQTESD GPETLLNANN SRPSCTESKD SAECVDNYDV
EDTKLHNNTE DVTGDIHHSA EEENENLDFD FDEYKKPINW DEFLKNDPIL ESIRAIFSKK
YDYKENPDHT ETSEEVETDP KEQSYNYFTK NDDFHDDTFN DRDKTKEETD SYEKKEAKES
EIVDKNYYPY DNKELFKHIF GKDKESDSDK ELDIDTEKEF LSRYFTKDVL HQLQDNSTAE
EDRQKEESRN REDIHKTLSK ILEKKDRFSR LDENLNKMIE KGEAIPIKYN NFWSLEYESP
RKRNKDNEQE TEDSKEEA
//
