ID F2PQ20_TRIEC Unreviewed; 493 AA.
AC F2PQ20;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TEQG_03021 {ECO:0000313|EMBL:EGE03988.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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DR EMBL; DS995730; EGE03988.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PQ20; -.
DR VEuPathDB; FungiDB:TEQG_03021; -.
DR eggNOG; KOG0684; Eukaryota.
DR HOGENOM; CLU_022195_8_0_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
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 CDD; cd11041; CYP503A1-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46206; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT BINDING 436
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 493 AA; 55518 MW; 871D2907C56311E2 CRC64;
MAGNEGDSSA ISLSWMIQVT SVPAYDYGVP AITIWKDSRA GTPSKKGKPW AVPLPGGSGD
MIVLPHHCGR EFFNLPKDNL SMRHMMSDEI NFNHILDAAW KVPVEAMQAC NKPSSLKKLE
PLIMKEAENS ISQVMGSSKS WNEDSIFNIS LQVLIDTGVL LVFHPGFGRD AGLSKKMGEY
VGQVEARTHL YESMPRIMGP LLEIFAPECH QIRSAIKSMK KTIVPELRRI LKQKRESPPT
NDDHFYASSM IEIALKKGPL SRNGVVKDEE HHIDMMADET MFMFFEAVEP TTMILAAFIA
RFLRHREFLE PVRLELEQAL KLNDGKWNFD LFNHTPRFES FSREVLRMDC INMVAGSRQI
VKEPVTIKSL GMTFGPGTNL TTSGAFTHLD PEFYPDPTRF DGNRFYKPDS TASDIFRDTI
SPNEQWVSFG LGISSCPARL LGTRLCQLVA AKILLGYHIE LAHEDGKCPD FNVYVDAVGI
LNPEIRMRYK SRQ
//
