ID F2PJ90_TRIEC Unreviewed; 383 AA.
AC F2PJ90;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Reticulon-4-interacting protein 1 {ECO:0000313|EMBL:EGE01957.1};
GN ORFNames=TEQG_00998 {ECO:0000313|EMBL:EGE01957.1};
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).
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DR EMBL; DS995720; EGE01957.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PJ90; -.
DR VEuPathDB; FungiDB:TEQG_00998; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_3_3_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05289; MDR_like_2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43482; PROTEIN AST1-RELATED; 1.
DR PANTHER; PTHR43482:SF1; PROTEIN AST1-RELATED; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
FT DOMAIN 29..380
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 42282 MW; 44D080966B2E59CC CRC64;
MADQEHIPPF MPAVHLPPGP YDPSSPPPAS SLIYDPKFPT PQPNPSQYLI KVLSTALCRD
ELTWPEVISN SRFYQPPIPG YDVCGTILST PSDDEHTYDG PKFKVGDEVF GWLSVHRGGG
AADCALAEEN ELAFKPKNIT SVEAASIPLS AMTAWQAFFA HGNLKHIADK CGHLDSEVVR
DDCMDENGEE AKQLQPRIEP VRVLITNASG GVGVQALQLL RSKTLFGDQK FWICGTCSSR
NTAFLKDTLH IDEVIDYTVN PDLSEAFRSK GWQPVDFVFD CIGGQSLKQA HSPAVICDNG
SIVSVAHPLK EEWGDLGIEK RGLSSRYFII ELNGKQLEKI GTLVEKGEVR GFVDRVFELH
RAREAMELVE SKRVRGKVVL KVN
//
