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Database: UniProt
Entry: H0EW23_GLAL7
LinkDB: H0EW23_GLAL7
Original site: H0EW23_GLAL7 
ID   H0EW23_GLAL7            Unreviewed;      1119 AA.
AC   H0EW23;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Putative [NU+] prion formation protein 1 {ECO:0000313|EMBL:EHK97269.1};
GN   ORFNames=M7I_6999 {ECO:0000313|EMBL:EHK97269.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK97269.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHK97269.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC       EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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:EHK97269.1}.
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DR   EMBL; AGUE01000200; EHK97269.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0EW23; -.
DR   HOGENOM; CLU_002848_0_1_1; -.
DR   InParanoid; H0EW23; -.
DR   Proteomes; UP000005446; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR   CDD; cd03221; ABCF_EF-3; 1.
DR   CDD; cd18626; CD_eEF3; 1.
DR   Gene3D; 2.40.50.990; -; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR015688; eEF3_ABC2_chromodomain-like.
DR   InterPro; IPR047038; eEF3_chromodomain-like_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 1; 1.
DR   PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF00385; Chromo; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   Amyloid {ECO:0000313|EMBL:EHK97269.1};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Prion {ECO:0000313|EMBL:EHK97269.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005446}.
FT   DOMAIN          473..690
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          718..1035
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1024..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1071
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1119 AA;  122941 MW;  CB36976DE6CBF93A CRC64;
     MPTMIAKGEG PVPTQQEVSA ILDAIFTAPS SDASIASAYT LCDLLLNSVG FRGLSEYGIL
     TEIKKAAADK KSGLKRESAQ NLLGALFERF PPQQKISEVV LLLQDGGMVA CALDALADKG
     AVVRDAAQYG LDELFKGLSS EALVVGLLPV LTTYLAKRSG KWQGTVGGLK MLQKMADQAK
     MEIDDTKEVA NNKDLLREAM GIKLAGLIPV VEAGMHDLKS DVEKQAVITM NSMTALLSND
     DVAPRIPLLI KTMQNPSTDT LQKAIHALSQ TTFVSIVTSP VLALLTPLLE RSLNTPTTAQ
     EVLRQTVVVV ENLTKLVHDP IEARTFLPKL KPGVKGVQDR ASLPEVRNLA KRALDVIHKA
     MGEDDGVLAD GAIARTSADD VAKILDAQIK KAGGLSEDAD VFKLAKPYIC SMVAEDVNHR
     QIQRISTVVT PYLKHIMKEF NGAEAAGDGL QQFYVDEDHR KYGQPVKEDD GEIEIVNADF
     SLGYGGMLLL SHTNLRLLKG HRYGLCGRNG AGKSTLMRSI AKGQLQGFPS QDVLRTCFVE
     HNQGEAADIS ILEFVSRDPE IGDQGQKRII EVLSEVGFTS GPGGRQSEKV GSLSGGWKMK
     LALARAMLMK ADVLLLDEPT NHLDVANIAW LEHYLKTHTD ITSLIVSHDS SFLDNVCTDI
     YHYEPGKKLA CYKGNLAEFV KQKPEAKSYY TLSDSQVQFK FPPPGILTGV KSQTRAILRM
     NDCSYTYPGS NKPSLHNVTC QLTLSSRTAI IGGNGAGKST LIKLLTGETI PTSGTVEKHP
     NLRIGYIKQH ALEHVEMHLE KTPNQYLQWR YANGDDREVY MKQTRILSKE DQEQMDKMIN
     IGDGTGEKRI EAIMGRQKWK KTFQYEVKWV GMLPKYNTQI SRESLIKWGF NKLVQEFDDH
     EASREGLGFR ELSPKVISKH FEDLGLDPEI ADHNEISGLS GGQKVKVVLA GAMWNNPHLL
     VLDEPTNFLD RDSLGGLAVA IRDYKGGVVM ISHNEEFVGA LCPEQWHVAD GRVTHKGHLA
     VSADRFEDSK PNSGFNSSVQ SRTGSKATSR ASSVQSSAVN SAVNSGAEDN QDMSFRARKK
     KKKTKKELKD QEVRRRLRHI EWLNSPKGTP KYPDTDDDA
//
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