ID A0A0W8DIJ9_PHYNI Unreviewed; 1011 AA.
AC A0A0W8DIJ9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 30.
DE SubName: Full=ATP-binding Cassette (ABC) Superfamily {ECO:0000313|EMBL:KUF96159.1};
GN ORFNames=AM587_10008440 {ECO:0000313|EMBL:KUF96159.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF96159.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF96159.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KUF96159.1}.
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DR EMBL; LNFO01001031; KUF96159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8DIJ9; -.
DR STRING; 4790.A0A0W8DIJ9; -.
DR EnsemblProtists; KUF96159; KUF96159; AM587_10008440.
DR OMA; KVWHKEL; -.
DR Proteomes; UP000052943; 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; cd07346; ABC_6TM_exporters; 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; 1.
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:SF620; ABC TRANSPORTER; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KUF96159.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 82..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 309..593
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 631..869
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 111809 MW; 1243C460D73853BF CRC64;
MQRKAAAFEA TPVHSSLEMS SETTDFERVP PESSGGFVKI GGPLPDSSDP RTIKGASSAP
GNGHRLFYLR VIDSRKWHYS ETFALFLDFF VQVLAISFTQ KDSFHDEVAA KASRLFSSGL
MLCYFIDMVI RVLGLRLALF RSHSNIADLL CLVAMVVLLG SRYVMGDKEY WLCLGYLTIV
ACRLILKPRA RTFSKKLHKF RTNGDHIRIS IESLRASLAR IPGISAMSIE MMETDLVIIC
GRDEGDMTRD ELMNFLERAL HYRPPTLSAT EFLSHLRDID ASSSTLAYGI MDVVRSTLWH
WSTQIADLIF CFFVVCINAS VSPALAIFLA KLSDAFDTLD SGEPNESTLK FGVVGVLALC
VPFVLGDYAV GYFQSKMISK ATESMQSALL NIILRQDTQF FAERSEGDLN NLFSSDVARV
NALWQAVFWN LLNPLLAVVF GFSYALYMDV SIGIMSFAFT AVLLSSGPQG FAAQRSKEFG
SRNAYVAAEF QNAVGCEKVV RAYAIQDPLI TRFKKTCASL RKSQFSKDFW SSIVQIYIES
AMYIFVAIMT ASLAMKVWHK DLSSGEFFGF ITLLSRVSNP VTVLGGFMRV AIGNASSLQR
VDDIIVGLGS NSGKDENDKD MPPLPKMEHD LRVEKLVFKY DKASENYILN ELSATIPRGS
YTCVVGPSGC GKSTLLACLM QFQDADGGCI RLDGHDIFNF SKKSFMDQTA VVFQDGGILN
GTIYDNIRYG NISASNADCE EAARLAECHF IKNLKDGFET VVGQHATCNL SGGQAQRICL
ARALCRRPSL MLLDEATSAL DPETEASIVA TLERLSSKMN MTIISVTHRL STALNADQIL
VLNTGRVAEE GRYDALVQKG GLFYEMVHKV DKPEEEEDAA PVEKPDMVSM TKSRRRGTAP
RRNTDTIGAT GEEPKQMQDS ALALQQFTKT LSSRVAHDVG DGNRPAGTTS WYRYGNRNSH
RSRKTSDDGF TSRRSGNNSV EGGQWYPSQH DNRGAATSAA SEEERNKYFV L
//