ID A0A1S9D4P5_ASPOZ Unreviewed; 1114 AA.
AC A0A1S9D4P5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ABC transporter related protein {ECO:0000313|EMBL:OOO04052.1};
GN ORFNames=OAory_01048990 {ECO:0000313|EMBL:OOO04052.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO04052.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO04052.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO04052.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-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}.
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:OOO04052.1}.
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DR EMBL; MKZY01000011; OOO04052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9D4P5; -.
DR VEuPathDB; FungiDB:AO090009000567; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR OMA; EDHRKFG; -.
DR Proteomes; UP000190312; 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:UP000190312};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 472..696
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 716..1040
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1064..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 122368 MW; EC1914CF61D26097 CRC64;
MATAVSKTPS TVPPTPEEIS SLFNTIFTAE TSQQSLDASY ALTNLLIQSV GCLGFQKYDV
LSQVKKAASD KKNGARRESA MLIIGALFER FPREHPLSEV IFLLQDGGVL DIALDALADK
GAVVRDAAQY AIDALFAGLK PESMANGLLP ALSAYLSRGT GKWQGFVGAY SLIEKMAVKA
QMGNGTMEEE REKDILREAM GKTLKDLIPL VESGMHDLKA EVAKRACKAM NAVTTLLSND
DVAPRIPLLI KTMEQPSEKT LQDAIHALSQ TTFVAIVTSP VLALLTPLLE RSLNAPTTPQ
ETLRRTVVVV ENLTKLVHDP SEARTFLPKL IPGVQAVKDR ASLPEVRELA TRALSVMEKA
MSDSNVHAGS VTKTTPDEVL AVLDAQIQAN GGLAVPEAHT LFELGKTYIA EMVREDVNCR
MHDRIPICVA PYLRGLLPED KHDAVASALQ AHFIEEDHRK FGKPEPDDPN EVEIVNANFS
LAYGGMLLLN HTNLRLLKGH RYGLCGRNGA GKSTLMRSIA NEKLEGFPPQ DVVRTCFVEH
NQGEDADLSI IEYVSKDPKI AEAGQEHISQ VLLEFGFTDG PEGRQSQRVG SLSGGWKMKL
ALARAMLMKA DVLLLDEPTN HLDVANVKWL QEYLKKHTEI TSLIVSHDSG FLDEVCTDIY
HYENKKLVCY KGNLAAFVKQ KPEAKSYYTL SASAVQFKFP PPGILSGIKS QTRAILRMTN
CSYTYPGASK PSLTDASLTL TLSSRVAIIG GNGAGKSTFI KMLTGETIPQ TGKVEKHPNL
RIGYIKQHAL EHVEMHLEKT PSQYLQWRYA NGDDREVYLK QTRILTEEDK AQLEKPVDLK
DGRGPRRIEA LMGRQKWKKS FQYEVKWIGL LPKHNTMISR ETLLELGFFK LVQEFDDHEA
SREGLGFRNL EPPEISKHFE DVGLDPEIAN HNQISGLSGG QKVKVVLAGA MWNNPHLLVL
DEPTNFLDRD SLGGLAVAIR DFKGGVVMIS HNEEFVGALC PEQLHVADGR IVARTNTGVS
LDRFEDSAAN SPQTGTAVNS TATSAAASAA ASAAASAVNS GAEEQGELKF KARKKKKMTR
AQLKERETRR RLRHLEWLNS PKGTPRPPDT DDEA
//
