ID W9VSH7_9EURO Unreviewed; 1155 AA.
AC W9VSH7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Prostaglandin-endoperoxide synthase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O7_08066 {ECO:0000313|EMBL:EXJ55141.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ55141.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ55141.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ55141.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-2013) 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:EXJ55141.1}.
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DR EMBL; AMGW01000006; EXJ55141.1; -; Genomic_DNA.
DR RefSeq; XP_007760251.1; XM_007762061.1.
DR AlphaFoldDB; W9VSH7; -.
DR STRING; 1182544.W9VSH7; -.
DR GeneID; 19182636; -.
DR VEuPathDB; FungiDB:A1O7_08066; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000019473; 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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; cd20612; CYP_LDS-like_C; 1.
DR CDD; cd09817; linoleate_diol_synthase_like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR036396; Cyt_P450_sf.
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; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
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:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019473}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 405
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 1155 AA; 128672 MW; 7FB89A82C9F6D8D6 CRC64;
MVRKRKLSST SISAMNGSRD HPSDLDPVHT EFKITSTIKG FFESIAGSGP DPTNTVINGA
TVQSKPLLAR VLADIASQAP RIGENLGLIH SLVDTTLFDG GLVDDRQYQM EKILQLAASL
PPGSKSLDDL TDKFIKLLWE NLEHPPLSYQ GDEYKFRTAD GSNNNIMYPH LGKAGSYYAR
TVTPQTLQPG VLPDPGVIFD AIFARGEEPR EHPNKISSML FYLATIIIHD CFHTDDAQSG
KVKTSSYLDL APLYGSSQEE QNQIRTFKDG LLKPDTFSEK RILGFPPGVA AIVVCFNRFH
NYVAMQLKEI NEGGRFRAPK SDQDKVGLAK LDNDLFQTAR LVTCGLYVNI ILNDYVRTIL
NLNRTNSTWT LDPRKNFSDV FDSAGVPSGV GNQVSVEFNL VYRWHSAISI KDEKWTNDLY
QSLFPGRDVA SVTQWELLPR LKQWLDERGS DPSKWQLDSG KYKRTANGAF RDEDLVEILT
QSTEDVACAF GPRNVPLVMK LIDVLGIQQA RAWNVATLNE FRKFFKLQPH KTFSDITRNE
EVARSLKALY QHPDYVELYP GIVAEDAKDP LEPGSGLCPG YTISRTILAD AVALTRGDRF
YTVDYTPANL TNWGWSQVKS DPSVAQGGCF YTLLMRALPF YYRGNSVYAM FPLTVPEENR
KILTRLGVDH DYNFDPPSYV GVPTSIRSWK AVTDILADQG GFSVPWGPHT YYLTHHDYML
SGDSEANATQ RKETQSAMNC PVNGLAQVQK FYEDLTTQLV VARSERLRGE WYQLDACRDV
GNPSHAIFVA RMFHLPLKKR GDLNPIAVEV DQLYLALSIM FAYVFLDLDT ASSFKLRAGA
KTANEQLSKL VKIVCEAVKV GGMLRLGDIF STGIAGELLE DYGVHFLKRL FEGGKSVDVV
VSTIIPTAAA AVATQAQHFT QMLDIYLSPE HSEHWPEIQR CAWSNNPADF DKLKGYALEA
NRLAPAAFGL LRKANIDTTI VDNGQKVKVE SGDQIYVDFI TAGLDETVFP NPRTIDPTRD
RSLYVHQGHG PHSCLGRPMV EVAMAAQLKV FAKLKNLRRA PGPQGQLKKT IPAPNPTSSD
PKANPGRIEV FMLEDWSSWY PFPTTLKVHH EGLWREQPDQ LAGQTGVPGI QEDILDSDMA
ETNGLNGDYV EADTA
//
