ID A0A1W2TRE9_ROSNE Unreviewed; 1334 AA.
AC A0A1W2TRE9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE SubName: Full=Putative ABC multidrug transporter protein {ECO:0000313|EMBL:GAP91070.1};
GN ORFNames=SAMD00023353_1501990 {ECO:0000313|EMBL:GAP91070.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP91070.1};
RN [1] {ECO:0000313|EMBL:GAP91070.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP91070.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
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; DF977460; GAP91070.1; -; Genomic_DNA.
DR STRING; 77044.A0A1W2TRE9; -.
DR OMA; DLQWHES; -.
DR OrthoDB; 1067095at2759; -.
DR Proteomes; UP000054516; 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:SF219; 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:UP000054516};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 789..811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 865..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 978..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1014..1036
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..358
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 394..673
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 754..1042
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1090..1329
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1334 AA; 143249 MW; D92404A9F9E34143 CRC64;
MALNPEPGSN ASGTDGKEAN ATPSRASRII GSIFSYFHLL NYAEPTTLDY ALLGTGVVSA
IGAGIPFPIL GILFGELVDE LNGATCANEG DGGGSSQSPE EYLAAINQKI LLVVAAALAQ
FALIYIYSVC WNLFGERLAH RLREKYFRSL LRQEVSFFDK LPAGEVSSRL SADINTIKNG
TSEKVGVYLG VLSLFITSYV IAFIKGPKLA GILVSLVPAF LIMTFGGGHY VGKYATLASE
HIASASSIAL ESLSNVMVVH AFRANDRLEA KFAAKLGQAK KEGIKKATAV AIQSGLLYFI
AYAACGLAYW QGSIIIADVA AGRAEGVSVG SIYTIIFILV DASIVISQVS PYLQIFSSAA
AVLGKLKTDI DRESKIDGTI EDSAHPPEVF EGDVRMENVA FTYPSRPDVP VIQDVSLQFP
AGKTTAIVGL SGSGKSTVAG LLTRLYDTDD GNLFLDGRNI RDINVRQLRS YIGLVQQDPM
LLNRSVLENI ALGLVNSSRP EHAAFQPIVL GNQLAQVAEA VRGGQDILTA AAAYGQDMVE
IARMILHAAD LADAGAFLGN LEFGLGTAVG PNGELLSGGQ KQRVALARAV VKNPRILVLD
EATSSLDSAS EQRIQTAIEQ ASVGRTVISI AHRLATVKNA DKIVVMRNGR VIEQGTHSDL
MAKDADYAAL VRLQNMGSES SSISTAQGSK TSVDLQGKPD SILDSDLGEI ADGIESSKHE
AESKDPEKEE PTPSVWSTMK RMGSLTRPHL LWLFIAFFGS LIVGGTYLGS ALIFGNTIGA
LSPCNTEQMI RAAGSFFGLL YFVLAIVEFF ANGTSWSVFG LVAEKVLYVV RVLSFRSLFE
QDLQWHQSEN RTPSSLLSFI TSDTAAIGGL TGSIIGTMFS IFVNFLGAII LSHIVAWKIA
VVCLAVVPVM LGAGFMKLWI VARFDEKHGK AFEKSVGISV EAVNSIKTVA ALSLEQEILG
TYRRSLEVPR KEVTRSILWS NGFLALSMSI SNLLYALIYW WGSKQIVSGM YTQAQFFIVL
ISLLVSAQLW GQLFTLAPEI TRAGRAVGRI CDLIDLGSSD GTDKGLRDND PEAMVESRTP
VSAPGQGLAV KFKQVKFSYP ARPNRQVLKG LDIDIAPGQF CALVGPSGAG KSTIISLLER
MYSIESGAIE VGGFNINSRR DALFRDDIGL VPQDSVLFDG SVRFNVALGA RPGPEPTDAE
IEEACKLANI HETIVALPDG YDTQCGNNGG QLSGGQRQRL SIARALVRRP RLLLLDESTS
ALDAESERLL QDGLEKATRG ITVVAIAHRL HTIRRADVIF MVEDGRCVEK GSHEELMVRS
EGYRVNVLHQ TLDG
//
