ID A0A319CJR6_9EURO Unreviewed; 335 AA.
AC A0A319CJR6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Bax inhibitor family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO82DRAFT_330854 {ECO:0000313|EMBL:PYH84071.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH84071.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH84071.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH84071.1,
RC ECO:0000313|Proteomes:UP000248340};
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; KZ821686; PYH84071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CJR6; -.
DR STRING; 1448315.A0A319CJR6; -.
DR VEuPathDB; FungiDB:BO82DRAFT_330854; -.
DR OrthoDB; 1703953at2759; -.
DR Proteomes; UP000248340; 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:UP000248340};
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 80..99
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 119..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 239..258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
SQ SEQUENCE 335 AA; 37034 MW; 65DD86FA86F920B1 CRC64;
MAFFLRRPFA VPTALRQISK PANSARFIHN TPFKPAQPKP TGSFSSSIFA KSRQTFQNAF
RRTYMQQPTY NTRGELLQKL GYGAAIVGGT IIATNLIFNR ETREDGGMPH YERSYLNETF
MHTGLGVGII AIAARAMHMN GFSYRMMAAN PWLVMGLGLV ASIGTMYGTL YTSPDNYVVK
YGLWTAFNIT QAALLSPLMF MSPALLARAG LYTVGMMGSI AFVGATAKQE KYLYLGGPLL
AGVAIVALSG LAPMVLPVTA TRTLMWSEKI WLYGGLAVFG GFTLYDVQKI LHHARLSQRG
LVRKDVVNES ISLTLDFINI FVRMVQILGM RQQRK
//
