ID A0A318ZMM2_9EURO Unreviewed; 272 AA.
AC A0A318ZMM2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 02-APR-2025, entry version 16.
DE SubName: Full=Bax inhibitor family protein {ECO:0000313|EMBL:PYH48871.1};
GN ORFNames=BP01DRAFT_288806 {ECO:0000313|EMBL:PYH48871.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH48871.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH48871.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH48871.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KZ821220; PYH48871.1; -; Genomic_DNA.
DR RefSeq; XP_025434853.1; XM_025571552.1.
DR AlphaFoldDB; A0A318ZMM2; -.
DR STRING; 1450539.A0A318ZMM2; -.
DR GeneID; 37072780; -.
DR OrthoDB; 7933078at2759; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd10429; GAAP_like; 1.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; BAX INHIBITOR-RELATED; 1.
DR PANTHER; PTHR23291:SF50; PROTEIN LIFEGUARD 4; 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:UP000248349};
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 71..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 30874 MW; FF969D134BA9D391 CRC64;
MAANTRYEPA PQRDSFEERA YTQPPPSYQA TADYSQAPPR GEDDNVPDDF KFGGTVAEGT
LPIRMQFIRK VYAILTAQLL LTTVMSSISF FSPSYRNWIQ SNFWVMILSV FGALGFMLVT
YWKRKSYPAN LLFLSGFTIM EAYSISVVTS LYESRIVLQA LVITLGLFVA LTLFACQTKY
DFTHWMPYLF GALWFLILFG FMAMFFPGSK TVELIYGGVA ALVFAGYILV DTQLVMRHYH
VEEEIAASIS LYLDILNLFL AILRILNSQS NN
//
