ID A0A1R3R9R4_ASPC5 Unreviewed; 1117 AA.
AC A0A1R3R9R4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ABC transporter domain-containing protein {ECO:0000259|PROSITE:PS50893};
GN ORFNames=ASPCADRAFT_211501 {ECO:0000313|EMBL:OOF91218.1};
OS Aspergillus carbonarius (strain ITEM 5010).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=602072 {ECO:0000313|EMBL:OOF91218.1, ECO:0000313|Proteomes:UP000188318};
RN [1] {ECO:0000313|Proteomes:UP000188318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV907512; OOF91218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3R9R4; -.
DR STRING; 602072.A0A1R3R9R4; -.
DR VEuPathDB; FungiDB:ASPCADRAFT_211501; -.
DR OMA; EDHRKFG; -.
DR OrthoDB; 49929at2759; -.
DR Proteomes; UP000188318; 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 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 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:UP000188318};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 482..706
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..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1117 AA; 123324 MW; DC5D62D4AC053A95 CRC64;
MPHPESPTPA MTTVVSKTPS GIPPTAEEIA SIVNTIFNAD TSQQSLDAAY ALTNLLIQSV
GCSGFQKYNL LPEIKKAATD KKNGARRESA MLILGALFER FPREHPLSEV VFLLQDGGVL
NLALDLLADK GAVVRDAAQY AIDALFACLK AEALVNALLP AITAYLHQNT AKWQGFVGAY
SLIEKMATKA QMGAGTLEEE REKDVLREAM GKTLKDLIPL VESGMHDLKN EVAKKSIKAM
NAITTLLSND DVAPRIPLLI KTMEQPSEQT LQKAIHALSQ TTFVAIVTSP VLALLTPLLE
RSLNAPTTPQ ETLRQTVVVV ENLTKLVHDP AEARTFLPKL KPGVQRVKDR ASLPEVRDLA
TRALDVIEKA MADKDVAQGV VVKITPEEVM VVLEAKIQEH GGLARPEDAT LFALGKNYIA
EMVREDVNCR MHDRIPTCIA PYLRGLLQDG KQDEVAAAVQ EHFIEEDHRK FGKPIPDDPN
EVEIVNANFS LAYGGMLLLS HTNLRLLKGH RYGLCGRNGA GKSTLMRSIA NEKLEGFPPQ
SEVRTCFVEH NQGEDADLSI FEYVQKDPLI AKEGEEHIRS VLLEFGFTDG PEGRQNQRVG
SLSGGWKMKL ALARAMLQKA DVLLLDEPTN HLDVANVKWL QEYLKKHTDI TSLIVSHDSG
FLDEVCTDIY HYEQKKLVCY KGNLADFVKV KPEAKSYYTL SASIVQFKFP APGILSGIKS
NTRSILRMTN CTYTYPGASK PSLSDASLSL TLSSRVAIIG GNGAGKSTFI KMLTGETIPQ
TGKVEKHPNL RIGYIKQHAL EHVEMHLEKT PSQYLQWRYA NGDDREVHMK QTRILTEEDK
AQLEKPVDLG DGRGPRRIEA LIGRQKWKKS FQYEVKWIGL LPKHNTMISR ETLLNLGFFK
LIQEFDDHEA SREGLGFRVL DPKIISKHFE DVGLDPEIAN HNEISGLSGG QKVKVVLAGA
MWNNPHLLVL DEPTNFLDRD SLGGLAVAIR DFKGGVVMIS HNEEFVGALC PEQLHVADGR
IVSRTNTAVA LDRFEDSAAS SPQPGSTAVN STVTSAAASA VNSGAEEQGE LKFKARKKKK
LTRAQLKERE ARRRLRHLEW LQSPKGTPKP VDTDDEE
//
