ID B6Q7S4_TALMQ Unreviewed; 663 AA.
AC B6Q7S4;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Prostaglandin G/H synthase 2/cyclooxygenase 2, pgh2/cox2, putative {ECO:0000313|EMBL:EEA28809.1};
GN ORFNames=PMAA_036020 {ECO:0000313|EMBL:EEA28809.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28809.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995899; EEA28809.1; -; Genomic_DNA.
DR RefSeq; XP_002145324.1; XM_002145288.1.
DR AlphaFoldDB; B6Q7S4; -.
DR VEuPathDB; FungiDB:PMAA_036020; -.
DR HOGENOM; CLU_002329_2_1_1; -.
DR OrthoDB; 3322316at2759; -.
DR PhylomeDB; B6Q7S4; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09817; linoleate_diol_synthase_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 InterPro; IPR034812; Ppo-like_N.
DR PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 3.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT BINDING 379
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 663 AA; 75388 MW; EEA1FE073B67FB44 CRC64;
MESAAQFLGD IATNSKVILK GTKDHVDGII ADLHAVGLKT TAEDAQSLAT YLAQMKTGDG
VDDRAMRQEK LMSWLFKLPL EPKSAVGSTL EHGVVQSLWD TLPNPCPGWT QHSGPQYRRA
DGSFNNLYEP RVGRAGEAYI RNVVSLRDQS KDLPSPEDVF EKLFRRRTPA DGGFRKHPCG
ISANMFYMAT LITHDLFNTD ITNRFRNKTT SYVDMAWLYG KFHDCIGWNQ EMQDSVRDKA
GHCGKLHADV FADPRLDLQP PGVIAMALLW CRNHNWIAEQ LLIESKDDPR FSAVPKNDDQ
QGLELLDEHL FQTARNINVG TFATVVLKDY VRMLLGINRE NTTWTLPINQ EFSPSTKNDI
PKATGNQCSI EFNFIYRWHS AISVEDEQWI EGLFEDLEKR LGPNWMNNRL GSILPARIPA
FVQERHDERA STDPRCRTYF ALNPEVKRDP KTHKYPDAAL ADFIKRATES SAGAFGGRQV
PNVFKDIEIM SIRHARELGV CTLNELRTLC NLRPYRTFSE MNDNEAIATA LKDLYGDIAD
VELYRGLVAE QAKPRQEATG LCAGRTITYV ILSDAVALVR GDRFLTTELN PYNLTKWGYD
EIQPDNSWSF GNVLGDKLLN RHLGEENMPR DSIYTQYMFS TPEETTRNIK RFGMEKVYRE
TRL
//
