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}.
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; 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
//