ID A0A319CFW6_9EURO Unreviewed; 1116 AA.
AC A0A319CFW6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=BO82DRAFT_334062 {ECO:0000313|EMBL:PYH82217.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH82217.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH82217.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH82217.1,
RC ECO:0000313|Proteomes:UP000248340};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000256|ARBA:ARBA00011054}.
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DR EMBL; KZ821696; PYH82217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CFW6; -.
DR STRING; 1448315.A0A319CFW6; -.
DR VEuPathDB; FungiDB:BO82DRAFT_334062; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000248340; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 482..699
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 726..1043
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 122890 MW; 29781A988AB3577B CRC64;
MPHPESPTPA MQTAVSKTPS GVPPTYEEIG SLIHTIFNAE TSQQSLDAAY ALTNLLIQSV
GAAGFTHYNI LPQIQKAAVD KKNGALRESA MLILGAMFER FPREHPLSEV VFLLQDGGLL
HLALDLLADK GAVVREAAQY AIDALFACLK AEALANGLLP ALSAYLNRNT AKWQGFVGAY
ALIEKMAVKA QMGAGSLEEE REKDLLREAM GKTLKDLIPL VEAGMHDLKN EVAKQAIKSM
NAITTLLSND DVAPRIPLLI KTMEQPSEQT LQKAIHALSQ TTFVAIVTSP VLALLTPLLE
RSLNAPTTPQ ETLRQTVVVV ENLTKLVHDP AEARTFLPKL KPGVQRVKDR ASLPEVRELA
TRALDVIEKA MADKDVAAGV VVKITPEEVR TVLEAKIQEQ GGLAHPELVT LFELGKNYVA
EMVREDVNCR MLDRIPTCVG PYLRGLLAED KHDAVAAALE AHFIEEDHRK YGRPEPEDPN
EVEIVNANFS LAYGGMLLLS HTNLRLLKGH RYGLCGRNGA GKSTLMRSIA NDKLEGFPPQ
DVVRTCFVEH NQGEDADLSI YEFVVKDPKI AAEGEEHVRN VLLEFGFTDG PEGRQNQRVG
SLSGGWKMKL ALARAMLLKA DVLLLDEPTN HLDVANVKWL QEYLKAHTEI TSLIVSHDSG
FLDEVCTDIY HYEQKKLVCY KGNLADFVKV KPEAKSYYTL SASNVQFKFP PPGILSGIKS
NTRSILRMTD CSYTYPGASK PSLTGASLSL TLSSRVAIIG GNGAGKSTFI KMLTGETIPQ
TGKVEKHPNL RIGYIKQHAL EHVEMHLEKT PSQYLQWRYA NGDDREVHLK QTRILTEQDK
AQLEKPVDLG DGRGPRRIEA LMGRQKWKKS FQYEVKWIGL LPKHNTMISR ETLTELGFAK
LVQEFDDHEA SREGLGFRIL EPKIIAKHFE DVGLDPEIAA HNQISGLSGG QKVKVVLAGA
MWNNPHLLVL DEPTNFLDRD SLGGLAVAIR DFKGGVVMIS HNEEFVGALC PEQLHIADGR
IVGRTNNAVA LDRFEDSATS TPQPGSTAAN SATTSAAASA VNSGAEEGEL KFKARKKKKM
TRAQMKEREA RRRLRHLEWL QSPKGTPKPP DTDDEE
//
