ID A0A444XA79_ARAHY Unreviewed; 1627 AA.
AC A0A444XA79;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE RecName: Full=ABC-type xenobiotic transporter {ECO:0000256|ARBA:ARBA00012191};
DE EC=7.6.2.2 {ECO:0000256|ARBA:ARBA00012191};
GN ORFNames=Ahy_B10g106219 {ECO:0000313|EMBL:RYQ86552.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ86552.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ86552.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ86552.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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}.
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:RYQ86552.1}.
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DR EMBL; SDMP01000020; RYQ86552.1; -; Genomic_DNA.
DR STRING; 3818.A0A444XA79; -.
DR Proteomes; UP000289738; Chromosome b10.
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; 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:SF375; ABC TRANSPORTER C FAMILY MEMBER 11-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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000289738};
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 31..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 920..944
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..989
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1065..1084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1157..1174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1180..1204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..593
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 627..849
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 929..1212
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1249..1483
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 1627 AA; 183302 MW; 52B7F2A980397C4E CRC64;
MEPFVWYCKP ESNSVWAKAV DSAFGSYTPC AINTLVISTS NFVLMGLCFY RIWLIATNTK
AQRFSLRSNW YNYVLALLAS YCAIQPLLRL LTGISAFNLN GETGFAPFEA MALIVEALTW
CSMIVLILLE TKVYIRQFRW VVRFGVIYVL VGDVVLLNLL LSVKDYCSRS ALFLYLSTFI
CQVLFGTLLF VYVPNLVPYD GHITMQDELP DNAEYELLCG EEQVFPEMHA NIFSRLCFGW
VTPLMRQGYR KPIREKDVWK LDKCDQTETL TEKFQKCWML EFQSSNPWLL RSLNNSLGKR
FWWGGIYKIG NDLSQFVGPI LLNHLLNSMQ NQDPSWVGYI YAFSIFVGVS LGVLCEAQYF
QNVMRVGFQL RSTLVAAIFR KSLRLTNEGR KKFSSGKLMN MITTDANALQ QICQQLHGLW
SAPFRIIIAM VLLYQQLGVA SLIGSLMLVL IVPLQASLYM ISFTRVHTYV IAKMRKLTKE
GLQQTDKRVG IMHEILAAMD TVKCYAWETS FQCRVQSIRD YELSWFRKAH LLNALNTFIL
NSIPVLVTVT SFGMFTLLGG ELTPARAFTS LSLFTVLRFP LNMLPNLLSQ VANANVSLQR
LEELFLAEER NLKQNPPLVP GLPAISIKNG NFSWDAKAEK STLSNINVEI PIGSLVAIVG
GTGEGKTSLI SAMIGELPLL KDGNAIIRGT VAYVPQISWI YNATVRENIL FGSEFEYERY
WKAIDVTALQ HDLNLLPARD FTEIGERGVN ISGGQKQRVS LARAVYSDSD VYIFDDPLSA
LDAHVAHEVF KNCIKEALGG KTRVLVTNQL HLLPQVDKII LLSDGMIKEQ GTFEELSKCG
YLFQRLMENA GKMEQQSESN EGREDHVEVN VSTSSNEALV QIPNDTSYEK KGKLRKSVLV
KQEERETGVV SLKVLARYKA ALGGLWVVFI LFACYTLTEV LRISSSTWLS VWTDQDSTSD
YNPVYFLVVY ALFSFGQVAV TLANSYWLII SNLRAAKRLH DAMLDKILRA PMVFFQTNPV
GRIINRFAKD MGDIDTMVST LVNQFMGQLW QLLSTFVLIG TVSTISLWAI MPLLIFFYGA
YIYYQSTARE VKRLDSITRS PVYAHFGEAL NGLASIRAYK AYDRMAHING KFMDKNIRFT
LVNISSNRWL TIRLESLGGL MIWFIATFAV LQNGRSENQA AFASTMGLLL SYTLNITSLL
SGVLRQASRA ENSLNAVERV GTYIDLETEA PRIIETNRPP PGWPTSGLVE FENVVLSYRP
ELPPVLHGLS FTVLPTEKVG VVGRTGAGKS SMLNALFRIV ELQSGRIIID GFDISMFGLA
DLRRVLTIIP QSPVLFSGTV RFNLDPFTEH NDADMWQALE RAHLKDVIRR NPLGLDAQVL
EGGDNFSVGQ RQLLSLARAL LRRSKVLVLD EATAAVDVRT DALIQKTIRQ EFQSCTMLII
AHRLNTVIDC NRILLLDSGR VLEYDSPDKL LSNEASAFYK MVQSTGAANA EYLCSLVFGR
IVNNSNEENK GLENQMRQLA SSNWAAATQC AIAATLSSLH LNLQSPNETK DNKDFLEKTK
DALTTLQEVL EGKHDDVIQQ TLVKYNVPTE RWWSTLYQLV EGLSVLIKLP PKNIQQLELD
FERRSFH
//
