ID   C7Z0G5_FUSV7            Unreviewed;      1101 AA.
AC   C7Z0G5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEU42377.1};
GN   ORFNames=NECHADRAFT_40259 {ECO:0000313|EMBL:EEU42377.1};
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122 {ECO:0000313|EMBL:EEU42377.1, ECO:0000313|Proteomes:UP000005206};
RN   [1] {ECO:0000313|EMBL:EEU42377.1, ECO:0000313|Proteomes:UP000005206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4
RC   {ECO:0000313|Proteomes:UP000005206};
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.J., Danchin E.G., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   Vanetten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; GG698905; EEU42377.1; -; Genomic_DNA.
DR   RefSeq; XP_003048090.1; XM_003048044.1.
DR   AlphaFoldDB; C7Z0G5; -.
DR   STRING; 660122.C7Z0G5; -.
DR   EnsemblFungi; NechaT40259; NechaP40259; NechaG40259.
DR   GeneID; 9667262; -.
DR   KEGG; nhe:NECHADRAFT_40259; -.
DR   VEuPathDB; FungiDB:NECHADRAFT_40259; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   InParanoid; C7Z0G5; -.
DR   OMA; RHYTIDY; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000005206; 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; IPR001128; Cyt_P450.
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   Pfam; PF00067; p450; 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:ARBA00022964};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005206}.
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         408
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   1101 AA;  123771 MW;  6C7D740427B3F963 CRC64;
     MSSAEVKNGH ATNGHSQEKA PAPKPQPKAA GQSNQKKEGA LKSFKKLRVL SKRPLPTEMG
     DGSYRTVVNR PRLKEDLRRL KIKDLKTLLE IVKAKAKGET QQDDKTMIME RTIQIVASLN
     DHSKVQEVLT NSFIDKLWNS LDHPPMLYMG DQYRFRQPDG SLNNPYMPKL GAAKTPYSRS
     VRPKGMSLGA QPDPEAVFES VMARDGFKKN PNNVSSILWY WATIIIHDLF WTNLKDPNQN
     DSSSYLDLSP LYGSTVEARD SIRTFEDGLL KPDTFADKRL IGNPPGVCII LIMFNRFHNH
     VATNLADINE GGRFSKPGPN LDPEAAAAAW KKRDEELFET ARLVTSGLYI NITLIDYVRN
     IINLNRVDTT WTLDPRQEMG VSVGTKEGSE SGTGNVVSAE FNLCYRWHSC ISEMDDKWIQ
     DFYVQLLGDN YGAMDMRALM MALKKFEMSV PQDPAERTFG GFKRGKDGKF SDNELVDALA
     TAIEQPGGAF GGRNVPRIMK PVEMLGIIRG RKWNLAGLNE FRKHFGLKAY DTFEEINSDP
     EIAESLRNLY QHPDYVELYP GIVAEEAKTP MVPGVGIAPT YTISRVVLSD AVALVRGDRY
     YTTDYHPRNL TNWGYKEVDY DLNINHGCVF YKLFIRAFPQ HFKGNSVYAH YPMVIPSENR
     KILTDLKRAD RFDFDRPSFT PARINIVGYN AAKYILENQE IYKVCWDEGL GHLMGEGGRR
     FMLSGDGAFF AQQRRCMGAL LYNDTWKSAI KSFYSMIAEK LLAEKSYKLA GKTQVDVVRD
     VGNLAHTHFV SRMFNLPLKT KENPKGLFSE QELYKILAVI FVCIFFDIDP AKSFPLRQGA
     REVAQALGKV VEMNVKLSNG IGMKGLFTGK ANKDDPLAAY GVNMAKGLKK AGLSTEDIVW
     SQILPTAGAM VPNQAQVFAQ TLDWYLSPAG EKYRPELHRI AALETGDETD ALLLGYAMEG
     IRMAGTFGLY RKAESADVIE EDNGERVEVK AGDRVFVSFV SAAKDPKIFP NPEVVDPRRP
     LESYIHYGTG PHECLGRNIS QVALTELFRA LFRKKGLRRV PGAQGELKKV PRPGGFYVYM
     TEDWGSIWPF PTSMKVTWDG E
//