ID   A0A0M8N5J2_9HYPO        Unreviewed;      1110 AA.
AC   A0A0M8N5J2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Prion formation protein 1 {ECO:0000313|EMBL:KOS21104.1};
GN   ORFNames=ESCO_004071 {ECO:0000313|EMBL:KOS21104.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS21104.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS21104.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS21104.1}.
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DR   EMBL; LGSR01000013; KOS21104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8N5J2; -.
DR   STRING; 150374.A0A0M8N5J2; -.
DR   OrthoDB; 49929at2759; -.
DR   Proteomes; UP000053831; 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 3; 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:KOS21104.1};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Prion {ECO:0000313|EMBL:KOS21104.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT   DOMAIN          474..691
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          719..1036
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1086..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1110 AA;  122133 MW;  C3E5571F1171C15F CRC64;
     MPHHVSPPTV VSDGAPPAPS KEDVAAFLNT IFTAQTSAAS IDASYGLCEV LLGSVGSAGL
     QYYGILDEVK KAAADKKSGL RRESSQNLLG AIFERFPARQ RLSEVLLLAP TAGAVACALD
     ALADKGSVVR EAAQYGLDAL FASLSAEALV TGLLPLLTDY LSRKTGKWQG TVGAYQMLQK
     MADKAQMTVG CTKEEALEKD VLREAMGAKL ATLIPIVEGG MHDLKAEVEK QAVRTMTSIT
     ALLSNDDVAP RIPLLIDTMQ HPSAQSLQKA IHALSMTTFV AVVTSPVLAL LTPFLERSLN
     TPTTPQEVLR QSVVIVENLT KLVHDPIEAR TFLPKLIPGV KAVCDRASLP EVREIGERAL
     ATMQKAMGND QDIVARLTTD DVAKLLDEQI QKNNGLVAYP DIFKLAKPYI CDMVATDANY
     RFVNRIFDRI APYLANLLIN AELVQPIAEA IQTHFVEEDE RRYGVPEKED DGEIEIVNAD
     FSLAYGGMLL LSHTNLRLLK GHRYGLCGRN GAGKSTLMRS IANGKLEGFP SQDVLRTCYV
     EHNQGEDADI SILEFVAKDP EIGPQGNEHI SEVLTEFGFT AGPEGRQSHK VGSLSGGWKM
     KLALARAMLK KADVLLLDEP TNHLDVANIA WLENYLKTHP DITSLIVSHD SGFLDNVTTD
     IYHYEPNKKL ACYKGNLAAF VKLRPEAKSY YTLSASQVQF KFPPPGILSG IKSMTRAIIR
     MTNVSYTYPK ATKPSLQDVS CQLTLSSRVA IIGPNGAGKS TLIKLLTGET IPSTGKVEKH
     PNLRIGYIKQ HALEHVEMHL EKTPNQYLQW RYQHGDDREV HMKQTRVLSD KDREQMDKPV
     DLKDGKAPRQ VELLVGRQKY KKTFQYEVKW RGLMPKHNTM ISRETLLELG FDKLVQEFDD
     HEASREGLGY RELQPAVISK HFEDLGLDPE IANHNEIGSL SGGQKVKVVI AGAMWNNPHM
     LVLDEPTNFL DRDSLGGLAV AIREFKGGVI LISHNEEFVG ALCSEQWHVN DGRVAQRGNA
     AVDLGRFEDS RPGSTVASTA VSTAANSVVS SAVNSGAEDN GELKFKARKK KKMTKKELKE
     REVRRRLRHI EWLNSPKGTP HPPDTDDEAE
//