ID G0S322_CHATD Unreviewed; 1089 AA.
AC G0S322;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Fatty acid oxygenase-like protein {ECO:0000313|EMBL:EGS22405.1};
GN ORFNames=CTHT_0019380 {ECO:0000313|EMBL:EGS22405.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS22405.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL988040; EGS22405.1; -; Genomic_DNA.
DR RefSeq; XP_006692424.1; XM_006692361.1.
DR AlphaFoldDB; G0S322; -.
DR STRING; 759272.G0S322; -.
DR GeneID; 18255976; -.
DR KEGG; cthr:CTHT_0019380; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_1_0_1; -.
DR OMA; RHYTIDY; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000008066; 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:0006979; P:response to oxidative stress; IEA:InterPro.
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:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 421
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 1089 AA; 121403 MW; 78EC0201DE0937CD CRC64;
MNGAKVTASR HASNGREKAP QEGREKLASK AKPKPTPRKV MPTKSDKEGV ANALERCAQI
FQATIKPAPN QEGPGPVNEP RKWGKLKQDL KTLRSADIKT LKQVVLARVK GEKLTDDKTM
IMERVIQLVA NLPNDSKLRV ELTNTFLGEL WNSLGHPPSL YVGDKYRYRQ ADGSYNNIMF
PQLGAAGSPY ARSVNTTVLR KGALPDPGLV FDSVMKRTEY KKHPNNVSSI LWYWASIVIH
DLFWTDHHDV SRSKTSSYLD LSPLYGSNQE MQNTIRTFKD GKLKPDCFAD KRIHGLPPGV
GVLLIMFNRF HNYVCDNLIS INEDGRFTAP SPSLQGDKAA AAWKKYDEDL FQTARLVTSG
LYINIMLLDY VRNIVNLNRV DTTWTLDPRV NTGIEADVRQ GAERGTGNVV SAEFNLCYRW
HSCISEKDEK WIEEFYWDLF GKPSAEVGVQ DLLAGFAMFE SRLPEDPLQR PFNKFKRGPD
GKFSDDDLVE CIVSAIEDCA GSFGARNVPA SMRAIEILGI IQGRKWNVAS LNEFRRHFGL
KPYETFEDIN SDPGVADALR RLYDHPDFVE LYPGIVAEER KEPMVPGVGI APTYTISRVV
LSDAVVLVRS DRHYTIDYSP RHLTNWGYND VQYDLNVNHG CVFYKLFLNA FPNHFNYNSV
YAHYPMVVPS ETEKIVKDLK RDHLFDFCRP GRLRKTAEVK EPEGVRHVLA GQEKYRGAWL
EALRPLADQG KAKLSGDAKT HDQLRQQVSE SVFDDDFVVT VKAFYRQKVA ELLDLRSYDL
AGNRMADLVR DVAALAPTYF VSELFGLPLE SRANKKGFYT EHELHVVLST IATVLFTQVD
VVKKFPLLQA VKTLSSQLAT AIEKTVKSPK SNKSQPLSSY GAKLIKALTK AGVSRHDITW
AHVLAASAAV VAYQTKIFTE AVDFYLSPAR AQFREAIQSL ATQPASEQVD SLLLGYALEG
IRLGGSTHLV FQAVAADTIP TVENSIEAGD FVTLNTSPSA CEPAQPDPSL HTHARSLYAH
LDASPDAVFL GGTAVRDATL VEFFRAVFCT QELAAHAGSA GRAEEGGGAR PDGQEHRTRA
VHARRLGRV
//