ID A0A372RJI2_9GLOM Unreviewed; 344 AA.
AC A0A372RJI2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Heme peroxidase {ECO:0000313|EMBL:RGB41003.1};
GN ORFNames=C1646_349731 {ECO:0000313|EMBL:RGB41003.1};
OS Rhizophagus sp. MUCL 43196.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB41003.1, ECO:0000313|Proteomes:UP000263633};
RN [1] {ECO:0000313|EMBL:RGB41003.1, ECO:0000313|Proteomes:UP000263633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB41003.1,
RC ECO:0000313|Proteomes:UP000263633};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGB41003.1}.
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DR EMBL; QKKE01000046; RGB41003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372RJI2; -.
DR STRING; 1803374.A0A372RJI2; -.
DR InParanoid; A0A372RJI2; -.
DR Proteomes; UP000263633; 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 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:SF4; LD42267P; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
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:RGB41003.1};
KW Peroxidase {ECO:0000313|EMBL:RGB41003.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..344
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016869154"
FT BINDING 340
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 344 AA; 38515 MW; C46B8545E1E2277C CRC64;
MLIRITSLIL LILCFIKTAV SQYDASNESF SYIREFPPDP FYPNGVGKML KTPMDSLPNN
AVPTVKCVDP LPIGAFPLPR CISNEFAYNL GPSINSNNLK RQSELRSRRR TNHMATWFGQ
YISFDITVSL TTIPSNPIYI PADDATFNPP SSIPGELSAK GVTSLPFNLS EVLPGTSDPL
NSVRNGVSLV SPLLDLDMVY GAYSAPDGTF NTIRNGTSCY LLTADNGKYP PKDDSGNYIK
SASTSSRSWT LFTMAINTVW IREHNRKCKE LFDTHGNSWT DQRYFEEARR WNIALYQKTV
SEEYLGTILG RPLPAYEGYK PDVYPGIDTF FATVSFRYGH SELR
//
