ID A0A0K0DU17_STRER Unreviewed; 1288 AA.
AC A0A0K0DU17;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=ABC transporter domain-containing protein {ECO:0000313|WBParaSite:SSTP_0000073300.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000073300.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000073300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A0K0DU17; -.
DR STRING; 6248.A0A0K0DU17; -.
DR WBParaSite; SSTP_0000073300.1; SSTP_0000073300.1; SSTP_0000073300.
DR Proteomes; UP000035681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF654; HALF TRANSPORTER (PGP RELATED); 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 725..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 770..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..863
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 869..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 950..974
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 994..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..334
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 369..605
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 726..1014
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1048..1284
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1288 AA; 144838 MW; 9FD339C206D47FD0 CRC64;
MTSSSDTTTI NDNKNSFFIV KIFSILRYAE TCDYILFILS VLLAMISGII QPFENIILGN
YFEAYLYGYK HFSEIQNSSR IVIVEEMAYK DTYNHALLSF IILITLFLSA ICSTVLIERQ
LKTMKKLYFK SVLRQDMMWF EKNPPGEIAT SLSTTFNKIR DGLNLKLTTF VSSSSYVMSS
IVISFQYNNI IGVSMFLSTV ITILPLIFGM YFHNRFEKKE LLYNSSIGAL VEEVLSGIKT
VITFNGQLFE IKRYLNGVNK LLEASKRKLI YLTGSCCIFY LFIYSQNAIY LYLFYNLFKN
ELIRFGSLIC ILFCSNGSAF RIQELTYQLL KFKEALYLTI NVLNVIDTIP EIDSLNMEGE
EIDNPTGSIT FDNVSFSYNS RPTESAIDSL SFKIEAGESC AIVGKSGSGK STIINLLMRF
YKVKSGEILI DGKSHEDLNI NWLRGITSVV SQDPVLFTGT VKENILLGNP TASDEEIYLA
CKMAHAHDFI NELPEKYNTQ IGEGKLKMSG GQKQRIAIAR ALVRKPKILI LDEATSALDA
SSEKYVQRAL NEACKGRTTL AVSHKIHSIK NYDKIIVLAH GKIVEYGNHN ELMDKKGEYY
KLFMCELQGL SCNKKNMYKS CDKNSISESN DDSLEVCRKK KSLIDNIVSK CMLPLDPNKV
FQKLTGIITK NDKKICSKGF SSTDPVIENC LNTLIKNQSK PEKVIAKKTS LLEIIKFSKN
EKKRFFIGMI FVLLKSLYYP CSVLIMGYIF KIFTLSFDNE IAKKKLTIAI ILVVASSLGN
SIIYAMCSYL IGLTGIRIGK NVRISAYTNI MRQDMTFFDN KSNGIGSLTK TLSSDALFFS
QGIDLSCIDA LVGILTIIIS IFFTLNSNII LGFTTISLII TVGLISYTLV TITHSILHKS
DIYEKKSINI GLECINNVKT IQCLSIIEGM SEKYFDSLNK IFKYKIKSGI LYASSFSLGY
SSVIQANALA FGAGSKLITR RLATPYDIIM GCQYINYISF SFCLINPYIV DYISFRIAAT
KLFKIIETKP KFDNLSNKGK TTPILGKIKM KSGYFSYPHI SNSLILKDMT FQIDYGDNLT
LVGLSGSGKS TTIQVIDRLY DLLDGILEID DVNVKDYNIR HYRNAVSVVS QEPTLFDLTI
KENICYGMEN VSDEELYNAA SIANIHKFIE SLPKKYDTPV GIKGRNFSGG ERQRISIARA
LVRKPNILLL DEATSALDNV NSTDVEMALT KAKLGRTCIS ISHKLNSAVN STFIGYVENG
KIVEFGNHES LMEKKGLYYT LVQQQQLD
//
