ID A0A165N0B5_9APHY Unreviewed; 281 AA.
AC A0A165N0B5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=UPF0005-domain-containing protein {ECO:0000313|EMBL:KZT66348.1};
GN ORFNames=DAEQUDRAFT_813587 {ECO:0000313|EMBL:KZT66348.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT66348.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT66348.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT66348.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV429090; KZT66348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165N0B5; -.
DR STRING; 1314783.A0A165N0B5; -.
DR OrthoDB; 944911at2759; -.
DR Proteomes; UP000076727; 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: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:UP000076727};
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 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 138..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT TRANSMEM 254..275
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004379"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 31053 MW; FF0D02E91A19856E CRC64;
MSTDHYTAPP PAYNTGPKLS KVPGDEEATQ PLLSPTAGPS SGPGGIYDQP GFDDIPDDFK
YGTTVSDSAL EIRNAFVRKV YSILFCQILA TCIVAGGISR SDETIFWVQT HMWSFYIPLF
GTLINLGLLF WKRHSHPANL ILLSTFTLFE AFTLGVTVAF FNPTIVLQAL LITLGVFLGL
TLFTLQSKYD FSGMGGWLFG GLVALMMTGL VGIFIPFSRT MDMIYAGGGC LLFSGYVVFD
TYMITKRLSP DEYIMAAISL YLDFINLFIN ILRLLNDMNR D
//
