ID A0A395N5X5_9HYPO Unreviewed; 340 AA.
AC A0A395N5X5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Bax inhibitor family protein {ECO:0000313|EMBL:RFN55522.1};
GN ORFNames=FIE12Z_168 {ECO:0000313|EMBL:RFN55522.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN55522.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN55522.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN55522.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000256|RuleBase:RU004379}.
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:RFN55522.1}.
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DR EMBL; PXXK01000005; RFN55522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395N5X5; -.
DR STRING; 2594813.A0A395N5X5; -.
DR Proteomes; UP000265631; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; BAX INHIBITOR-RELATED; 1.
DR PANTHER; PTHR23291:SF129; GROWTH HORMONE-INDUCIBLE TRANSMEMBRANE PROTEIN-RELATED; 1.
DR Pfam; PF01027; Bax1-I; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004379};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU004379};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU004379}.
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 122..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 236..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 274..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
SQ SEQUENCE 340 AA; 36803 MW; 556EBCA3B775B249 CRC64;
MSFTLTVRQG PARLAQRLPE LSKTAFRNAA SARSFHVQAK PSANFFSSRI TPATRNAFQR
SGRRSYNQQA PAVTTPQSAS RRLLVGGAIF GGTLVAINAV FNRETREDGG MPVYEREYLN
NTFLHTGLGI GIIGLTARQM VQTGFVYRIM VTNPWVVGIG GLALSFATMI GTRSISPDNY
LPKYALWTAF NATQAAFVAP LLAFCPPALL GRAGLYTIAM MGGLAVVGAT AKQEKYLYIG
GPLLAGAAIV AASGLAPLVI PATAVRTLAF TESLWLYGGL AVFGGFTLYD VQKVLHHARL
AQAGVIRRDP VNESISLELD FLNIFIRMVQ ILMMQQNRRK
//
