ID A0A0M8ZUX8_9HYME Unreviewed; 1438 AA.
AC A0A0M8ZUX8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peroxidasin {ECO:0000313|EMBL:KOX71477.1};
GN ORFNames=WN51_03649 {ECO:0000313|EMBL:KOX71477.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX71477.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX71477.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX71477.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX71477.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ435837; KOX71477.1; -; Genomic_DNA.
DR STRING; 166423.A0A0M8ZUX8; -.
DR OrthoDB; 4560at2759; -.
DR Proteomes; UP000053105; 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 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: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:UP000053105}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 606
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 1438 AA; 162059 MW; 27F0FDB19B8E5D51 CRC64;
MIQFDFTRDG NDEAVGTQNG QHTGIIRSGV NRSTAIGAIK CGKHAGMQMR TCSGKRVLLV
LLSSGLSKSA TNYEIPQSSD AKLSSAVRPT NDPTFHESNQ DDPEPIETLF IPEDPSEYER
ILLYVRRLFQ PAEESIDSFD REVPKDLGKH PIDDEDRFSR LEDVRGRDSG PSEREEGEEK
YLQRNPEGGV SPRTTTESNR KDEVVSMERR NYDASYDEKD EPDEKDLLEA ANFGLDAMRD
LYNIKEPMLY SMGLYLDSDN PARHLAVFND QTEEARTLAK FPNTPADSLL SRRSQSNPLR
RNCPNRGVPN CPAASLRYRT SDGSCNNLQH LWWGSAMSTM QRLLPPVYDD GIQSIRKSVT
GRPLPSARLV STVIHEDKDI PLESVTHMLM QWGQFVDHDL TATGQSRGFN GTVPQCCLKH
PECLPISVST QDKQLSQVTS YLDASAVYSS NAFQSDALRL FRNGLLQYGK IESQRPVLPK
LDSDLCRRGS LSTNCFRAGD GRLGEQPALT SLHVAFLRLH NRIATKLAAL NAHWSDEKLF
QESRRIVAAI VQHITYREFL PIVLGQSVMK IFDLELLKKG YYKGYDPTVN PTIANGFSTA
AYRFGHSLVQ QSFVRFTSDH QPIFNNVSIH NEFTNPVNLE TAGSVDRLIL GLINQNAQRR
DEHINEELTN HLFQTPSFPF GMDLASINIQ RGRDHGIPPY VQWRKPCALS PIKNFDDLER
AVPPSAVTKL RSVYSSVEDI DLFTGGLAEK SVRGGLVGPT FACIIGQQFS NIRRGDRFWY
ENSRQEGSFT PGQLQQIRRV TLAQVLCATM DNIETLQPFV FLTQDTLKNQ RVSCNDPVIG
QLNLQFWAER LPEFKRLGIF DKIKKNTSTN ANAPANSSTN NLNPPKTNVH QQNKIVVKKP
FGPSDNVTII VQNNAINSPV FLNDAIHGSS IMVNPSLNQQ TQQNAVPTFP PMRPVIITHP
LGGPIFKNDI YVPYAFRDPN NPNPLSQGYR SGYDSDVVFD SFPGSSPRPT LYTYYTTFQK
MTTQRPPQDV NAYTVNYKPQ DHGSKFASSR PNSQYQSQLW LKPVYASLEN NTDQENRINI
WQKVQYRPVV SVNQQASSNL LSYTSENPQN YLKNTEDKYV SSSQQDYSSN QQVYSNDSAN
KHTTWPSVSF DKKTEDKVTN DQHYRPYQKP TEIDYASSYQ TEFPIRPTTS LNNKGSSTIN
PNTVHINSSA RPVTSDEESN GSHNTISHST PIYRPAQQIS DYLASKPGNF YQTVKPSKIH
SVTIVTESTV SEGERDIDRI GNRVTSIPRP LVHQAGNNRV RKPGQYYYEK NVLHRYPDKI
DDQTDYNAEQ RHKTTSNETL IDQILSETSV RNHQVIDGNR NNTDVEIMDH TINESFDGAV
KNELAESTRG QKSTISSGNA KNPIKQNHCR QGTTKTHEAQ KLRLLTISPL TISISRYQ
//
