ID A0A0K0EFG7_STRER Unreviewed; 1624 AA.
AC A0A0K0EFG7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=ABC transporter domain-containing protein {ECO:0000313|WBParaSite:SSTP_0000823000.1};
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_0000823000.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000823000.1}
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; A0A0K0EFG7; -.
DR STRING; 6248.A0A0K0EFG7; -.
DR WBParaSite; SSTP_0000823000.1; SSTP_0000823000.1; SSTP_0000823000.
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 CDD; cd03263; ABC_subfamily_A; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF269; ABC TRANSPORTER CED-7; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF12698; ABC2_membrane_3; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
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 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 Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1624
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005328202"
FT TRANSMEM 277..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 873..893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 980..999
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1036..1059
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1080..1101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1113..1135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1218..1235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 494..735
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 1290..1513
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1624 AA; 185547 MW; 59E61A782C8D2CAD CRC64;
MFCAHLFLLL YKNLIVLWRS KKYVIPQNGS VVVKPHIFKN VSVLGNEIDT NLHIQMLPKI
WSQCFERRKA IVMYTLSDSI LTNNSELLLE EFEKRYSNKV SLMKMNSEKE ILDVYKNKYK
NDSYNCNPYI VSIHFQNISE KDGLHYKFIQ PSLPDHQWME KTQWIDGDVF GRSPDYFTLP
KQPPYWSSGL VTFQVALNEI FLTKFMKNIN IPTLSLQRMP LPEFHDDVIF SFISKIPLLW
LFVLTFTIIH TARDVVAERE SKMKAYLHAN GVKAIPWFLS HFIITLSKMY INIIIMSIPL
VIILNASSSA IFYIIILSFG FSLACFTLFI TSFCKTSTTI TSITILVIAL MHVFSSIYVP
NRFQKGLCFL YSLNIIGAFN FAITIFCHVE NSSKPFTVWD LFQLTNNNSS FSLSNAIFML
ILDGWIMLFL TFLLDALFPK DDSIPMSFKQ FLSTYLPIKF NYKNEYDRIS LSTSDSESET
IRESELIWNE NAILEVKNLV KSWKASGGNA VDGISFSVKK GNTSVLLGHN GAGKSTTFAM
LTGITAPTYG EIKLFGKHLY ENLDQFRKNI GYCPQDNPIF NNLTVGEQLK FIVLLKKGIF
GKITGRLSKE NRNYCDVVGF LERLKLIDKV NEYCNKLSGG MKRKLSVCMA LCGGSEMVFL
DEPTSGMDVE ARQDVTSLLN EEKKLRAILL TTHYMDEADS MGDRIIIMGK GRILCDGTSD
FLKKRFGTGY QLTFSLDNNS GFVKENILAF VKRIIPKSEI NIKDTSGQFS LILPINEKHK
FSELFKGLEE NKENLQIKSF GLSLNTLEQV FLKVGELADG GEDETDSAVK YARLISSEND
YNRVFGIKLF YNQIIALIRK QLYYYRRNLF TNLMRYLPII LIFIGVELFL TFFRDLIVFE
KTINSNVGLL GPIKVPLQDV KSMNSPIIEN YYNYLKSYKK FKINILPPYK NMTNYIIKES
LIEPPFGIGA KMDGVSNSML LLFNGNAYHS IFYAIHVFFN VMANVKQDFI KTNVVVYDVE
RSTSGMDDSF DLARKMMVLI GFLFISLNNT LCSFIDILVD ERISKFKHQQ LLTKLNIVTY
WLSFFIFNFI TYSIIVLFYF ASSIILSVFT QQYGSFLLLC ILFYFATISF IYWISFLFEK
PSKANSVMVS FHQIIPVAMT IIINIIVFIK GTSINKNIDN GLKVLVPGYN FLDGLLKLKD
SNGNDDMFND KNNLDNNYIL FVVSGFINLL LLYIVQSKII RKFIYDLWNL IYLKSNNRCS
NFDNNTNDDD DDVSKEINWV NTVESAGLPL IVNNLTKNYG KFRAVNNLTF GVNEKDCFGL
LGINGAGKTS TFDMLTGTIL PTSGKAYIKN VSINNSPSIG YCPQFDALLP DLSGYEAMNI
LCQLNGFIDY KSRSIYALES VDMLIHSNKK FKKLSGGQKR KISLSIAIMA NAGMIFLDEP
TSGIDPKARR AIWNLLTEVR KQNQSILLTS HSMDECETLC TKIGFMNKGK LSHIGTSQHL
KSKFGSDYIL EIIFEKPTLQ ILNEINDIII SKFNCPSADV KILTNTLRWH IPKTNYTWSV
LYDFVEKLYL KYSYISPLET TSSMTSINGA PKGPSIKDYS ITQNSLEQVF LRLSAMHEKS
HRED
//
