ID A0A1L7WCD3_9HELO Unreviewed; 1391 AA.
AC A0A1L7WCD3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Related to multidrug resistance protein {ECO:0000313|EMBL:CZR50440.1};
GN ORFNames=PAC_00312 {ECO:0000313|EMBL:CZR50440.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR50440.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR50440.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR50440.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FJOG01000001; CZR50440.1; -; Genomic_DNA.
DR STRING; 576137.A0A1L7WCD3; -.
DR OrthoDB; 1067095at2759; -.
DR Proteomes; UP000184330; 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; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 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:SF213; ABC MULTIDRUG TRANSPORTER (EUROFUNG); 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 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:UP000184330};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 146..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..442
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 474..732
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 804..1090
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1129..1379
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 153726 MW; B7F66EA8E672042C CRC64;
MKRNSTLQDD EVPFLEDDEG SENGSQRRTS SASGSTFVQS DVPSERESHE AKTYTELTIR
SNEKHKFSGS RRVDLPVSPT SPTSANGSSD EEENEPLLED DVLGGDEKVK QAPQAEAKKP
FISAEYKIAF SHFLRIFSYS TRNDRFLLAA AATASILTGV TLPLMNVVFG ELVGVFGAFY
SPESGETEEI FMQIIDKYVF YIIYLFIARL FLSYIATLGF RMASIRISAS IRLAYLRALV
NQPISVLDTL PPGQTAAIIT ITANILQLGI SEKLSMFLQS LSLVITALAV AFYYNWLLTL
VTSSGLMFIV AFYFLTIPHL VKGLKEVEEA DKMSSSIASE VFEMIRMVAA CGAEWKMAER
YSGWVEESRR RGFLLSPIVA IQQAPAFFAI HATFALSFWY AIKLYLESAI SSVTAIIIIL
MSIMTIVTSI GGIAGPLTAA AHAAGASGIL HTIIDAPQPQ TIGIQNSEIL SQDVVLENVT
FAYPMRWDVK ILDNLSVRFP AGKITAIVGA SGSGKSTIVG LLERWYELDG HLPVEMIMPW
SKPGAITIGG QNIRETDLTW WRSQIGLVQQ EPFLFNTTIF KNVEYGLIGT QWEDASPGQK
RKLVEQACKE AFADEFISRL PEGYNTIAGD AGIKLSGGQR QRLAIARSIV KQPSILILDE
ATSSVDIHSE RIIQVALDRI SRNRTTITIA HRLSTIMGAD NIVVLKKGQV VQQGTHDQLM
ADTDGHYFGL AHAQQLSMAD DSMTTKGISD PEKQNEDEMV PLKLREEFET VTCSENPVIE
PKSFRGSFGL FLWEQKYQWR WYGLMILGAG GAGVAFPIHA FLFAKLISLF NFWGEYLRDQ
TSFWCLMLLF LGFGVAISYF TLGWSSNVVS FQITATYRKE YFQNTLTKPV SYHDHADNSV
GALTSRMASD PTQLQQLLGI NMAIVLIALF NITGSIAFSV YFGWKLALLS ICTSMPIILF
SGFLRLRYEM QFEKLNYAVF ADSSKFATEA IGAFRTVSSL TLESEICRRY ETLLRNHTTD
AFKKAKWSTF VFALSDSSAL ICMAFILWYG GQLLASHEYT PFQYLVVYLA VVQGSSSAGQ
SLSFGPNVAS AFAAANRIQS MRSSSQDRTA LHAEESSLNS EKTEGGVKIE LQNVSFKYPT
RNVAVLNAVN MTVEAGQFAA IVGPSGCGKT SIVSLLERFY NPQKGRILCN NHDISKSSLS
SYRSNISLVA QEAALFSGTI RENILLGVPS LPPSSCTSCA KKTEEDLDTR LHRACREAGI
HDFIISLPEG YDTAVGARGV ALSGGQKQRI AIARALIRGP KLLLLDEATS NLDSETERDV
MEVFEQKGRG ITRIVVAHRL ATVQNADVIF VMGEGRVVER GSHQELLRLK GLYWQMWVGR
ERLREGAIRN C
//
