ID A0A059C5P4_EUCGR Unreviewed; 1444 AA.
AC A0A059C5P4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ABC-type xenobiotic transporter {ECO:0000256|ARBA:ARBA00012191};
DE EC=7.6.2.2 {ECO:0000256|ARBA:ARBA00012191};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_E01721 {ECO:0000313|EMBL:KCW73260.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW73260.1};
RN [1] {ECO:0000313|EMBL:KCW73260.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW73260.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00034018};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily.
CC {ECO:0000256|ARBA:ARBA00009726}.
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DR EMBL; KK198757; KCW73260.1; -; Genomic_DNA.
DR EnsemblPlants; KCW73260; KCW73260; EUGRSUZ_E01721.
DR Gramene; KCW73260; KCW73260; EUGRSUZ_E01721.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; A0A059C5P4; -.
DR OMA; QWPANAT; -.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR CDD; cd18580; ABC_6TM_ABCC_D2; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR044726; ABCC_6TM_D2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF165; ABC TRANSPORTER C FAMILY MEMBER 15-RELATED; 1.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 914..936
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 957..984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1028..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1056..1075
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 290..571
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 605..828
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 917..1198
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1237..1444
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 845..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1444
FT /evidence="ECO:0000313|EMBL:KCW73260.1"
SQ SEQUENCE 1444 AA; 160929 MW; 8535CE7BCAB5A4EF CRC64;
MDSPCLKEQV SIILQLGFLG ILLLVSLRKL VHLLGNRSNA TDQATDRHMI CHKSGIIDRS
SIVCTALVLG THLLMLSMLV NGNDATCRSK TQAFSSAIMQ VVSWAVTLIV LYKIRREKYM
KFPWILRAWW MCNFLLSLFC TTLNINYIIK SHSHLRTRDL ANFMCLLAST GLFSISICGK
TGMVFSHADG MREPLLSEKV KKHSESKRES PYGKATLLQL ITFSWLNPLF AVGIKKPLEQ
NDVPDLDIKD SAAFSSHSFS NCIKQVKDND GAKNPSIYKA IFFFIRKKAA INALFAVVGA
GATYVGPYLI DDFVNFLTDK KSRSLESGYL LTLAFVGAKM VETTAQRQWT FGAHQLGLQL
RAALVSHIYK KGLVLSGQSR QSHTSGEIIN YMSVDVQRIT DLIYYLNLFL ILPIQISLAI
YILQTKLGLG SVAALAATFT VMACNIPLTR TQKKYQSKIM EAKDSRMKST SEVLRNMKTI
KLQAWDNQFL NKLESLRKIE YEWLWKSKRL GALSGFIFWG SPTFISIVTF GTCMLMGIEL
TAGRVLAALA TFQMLQDPIF SLPDLLNVLA QSKVSADRVA SYLQEDEIQQ NAIEYIPKNQ
TQFDIEIINA TFSWNPDLIT PTMSDIELKV KRGMKVAICG TVGSGKSSLL SCILGEIEKL
SGQVKISGTK AYVPQSPWIL SGNIRDNILF GNPYDPDKYD RTVQSCALVK DFELFSAGDL
TEIGERGINM SGGQKQRIQI ARAVYQDADI YLLDDPFSAV DAHTGTQLFA DCLMGMLKDK
TILYVTHQVE FLPAADLILV MRDGRIAQAG KFEDLLKQNI GFEVLVGAHS EALKSILTVE
NLSRTTQDPT ADGKSNKDFN STAEIQPREH DSEHDLSLDK SEKEGRLVQD EEREKGSLGK
EVYWSYLTTV KGGVLVLIIL LAQASFQILL VASNYWMAWV FPPTSDTEPV YKMDIILLVY
VLLAVGSSLC ILLRALLLAV AGLWTAQTLF TKMLHSVMRA PMALFDSTPT GRILSRASTD
QSVLDLEMAW SVGWCAFSII QLLGTIAVMS QVAWEVFVIF IPVTAICIWY QQYYIATARE
LARLSGIQRA PILHHFAESI AGAATIRAFD QEDRFTGGNL GLVDNHSRPW FYNVSTMEWL
SFRLDLLSNF VFAFSLVLLV SLPEGIIDPS IAGLAVTYGI TLSELQASVV WHLCNAENKM
ISFERILQYS NLASEAALLI EDSRPPSNWP ETGKICFRNL KIRYAEHLPS VLKNITCTFP
GRRKIGVVGR TGSGKSTLIQ AIFRTVEPRE GSIIIDDIDI SKIGLHDLRS RLSIIPQDPT
MFEGTVRGNL DPLEQFSDRE VWEALEKCQL GDIVRGKEEK LDFAVVENGE NWSAGQRQLF
CLGRALLKKS SILVLDEATA SVDSATDGVI QKIISQEFKN RTVVTIAHRI HTVIDSDLVL
VLSE
//
