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Database: UniProt
Entry: A0A2I2G2H3_9EURO
LinkDB: A0A2I2G2H3_9EURO
Original site: A0A2I2G2H3_9EURO 
ID   A0A2I2G2H3_9EURO        Unreviewed;       423 AA.
AC   A0A2I2G2H3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Band 7 domain-containing protein {ECO:0000259|Pfam:PF01145};
GN   ORFNames=P170DRAFT_438795 {ECO:0000313|EMBL:PLB47079.1};
OS   Aspergillus steynii IBT 23096.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB47079.1, ECO:0000313|Proteomes:UP000234275};
RN   [1] {ECO:0000313|EMBL:PLB47079.1, ECO:0000313|Proteomes:UP000234275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB47079.1,
RC   ECO:0000313|Proteomes:UP000234275};
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   -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.
CC       {ECO:0000256|ARBA:ARBA00007161, ECO:0000256|RuleBase:RU366054}.
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:PLB47079.1}.
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DR   EMBL; MSFO01000006; PLB47079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2G2H3; -.
DR   STRING; 1392250.A0A2I2G2H3; -.
DR   VEuPathDB; FungiDB:P170DRAFT_438795; -.
DR   OrthoDB; 5479983at2759; -.
DR   Proteomes; UP000234275; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd03399; SPFH_flotillin; 1.
DR   Gene3D; 3.30.479.30; Band 7 domain; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR027705; Flotillin_fam.
DR   PANTHER; PTHR13806:SF31; FLOTILLIN-LIKE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR13806; FLOTILLIN-RELATED; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT   DOMAIN          6..145
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|Pfam:PF01145"
FT   REGION          397..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          177..239
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   423 AA;  46839 MW;  6FB6352DD2C00CB6 CRC64;
     MTIEKLQFSL PAVFTIGPEN EYEALRKYAL LLSGSTAENN FAKKENISDN ERKGHVQDIV
     KGIIEGETRV IVSSMTMEEI FKERQVFKNK VIDNVQNELK QFGLKIYNAN VKELQDTPGS
     EYFAFLSRKA HEGALNQAKI DVAEARMRGE IGEAEKKGRT KQEISKIDAD TAVLETKRKA
     EKAKADSELK NRQTELDSGV QLAQIVAKRE TEVRDAELKK KVENKRAETE LERLRAEQVT
     KSKVERESAQ EKADAAFYTE QKAADARLYR QKVEADAAFY RQRQDADAAF YQQTREAEGM
     LEMSKAYGAL VNVLGGPQAF LQFRMLETGT YEKLAKANGA AINGLQPKIT TWSTGGKADE
     SGDGLGSIQN IMQSLPPLLS TIHDQTGISP PSWLAQMPPG SHVDGSHNAK AIKGHSVGSS
     PAN
//
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