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Database: UniProt
Entry: A0A2G9GZ13_9LAMI
LinkDB: A0A2G9GZ13_9LAMI
Original site: A0A2G9GZ13_9LAMI 
ID   A0A2G9GZ13_9LAMI        Unreviewed;      1252 AA.
AC   A0A2G9GZ13;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Multidrug/pheromone exporter, ABC superfamily {ECO:0000313|EMBL:PIN10250.1};
DE            EC=3.6.3.44 {ECO:0000313|EMBL:PIN10250.1};
GN   ORFNames=CDL12_17162 {ECO:0000313|EMBL:PIN10250.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN10250.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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:PIN10250.1}.
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DR   EMBL; NKXS01003276; PIN10250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9GZ13; -.
DR   STRING; 429701.A0A2G9GZ13; -.
DR   OrthoDB; 5487044at2759; -.
DR   Proteomes; UP000231279; 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   CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
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; PTHR24222:SF48; ABC TRANSMEMBRANE TYPE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24222; ABC TRANSPORTER B FAMILY; 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   Hydrolase {ECO:0000313|EMBL:PIN10250.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..85
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        246..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        681..710
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        722..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        802..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        828..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        905..928
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..309
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          344..580
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          682..969
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1006..1242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          588..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1252 AA;  137146 MW;  9B272BC140796085 CRC64;
     MGKNDGIFRY ADRVDKLLMF FGTLGSIGDG LQIPLMMFVL SDVINDYGKL NSEISTRSVD
     KYALRLLYVA IGVGLSAFIE GLCWARTAER QTSRMRLEYL KSVLKQEVGF FDSQAADSST
     TYQVVSTISS DSNTIQVTIG EKIPDCLAYM SSFFFCLIFA FTLSWKLTLA AIPFTLMFIV
     PGLGFGKMMM DVAMKTVESY AVAGGIAEQA ISSIRTVYSY VAEHQTLEKF SSALQTTMEL
     GIKQGFARGL MMGSMGVIYI SWGFQAWIGS LLVSKRGEKG GDIFVAGFNV LMGGLNILTA
     LPNLTAITEA KSAAIRITEM IDREPAIDSD DKKGKALSYV RGEIQFKGIY FSYPSRPATP
     ILQGLDLKVP AGRTIGLAGG SGCGKSTIIS LLQRFYDPIE GEILLDGHKI NRLHLKWLRS
     QMGLVNQEPI LFATSIKENI LFGKEGASME DVKNAAKAAN AHDFIVKLPD AYETQVGQFG
     VQLSGGQKQR IAIARALIRD PKIMLLDEAT SALDTESERI VQTAIEQASK GRTTIVIAHR
     LSAIKTANLI VVLKSGRVVE SGSHDELMQL NDGEYAKMVE LQQSVAANDN STNFNPHNER
     RSHHRMMNIP SSPTSVMSSP RTPSMNPFSP FSTSAPFSAP FSVQYEGEYD SDDEDLKQQP
     AYPAPSQWRL LKMNEPEWGR ALLGCLGAIG SGAVQPINAY CVGGLIAVYF RTDKSSITSH
     ARPYSLVFLG LGVFNFITNL AQHYNFAIMG EKLTKRVREM LLKKIMTFEI GWFDRDENTS
     AAITARLSTE ANMVRSLVGD RMSLLAQAIF GATFAYTLGL ILTWRLALVM MAAQPLLIGS
     FYMRSVLMKS MSAKAQIAQK EGSQLASEAV INHRTITAFS SQKRIVGLFR NTLEDPRKES
     IRQSWFAGVG LFSSQFLAAA STALAYWYGG RLLAQKLISP ERLFQAFLAL LFTAYTIAEA
     GSMTGDISRG TTAVGSVFAI LDRQSEIDPE SSQQTDEIKK GIRGRVELKK VVFAYPSRPE
     QLILKGLSLK ISAGTTVALV GQSGSGKSTI ISLIERFYDP LNGSVCIDDK DIKEYDLRTL
     RSHIALVSQE PTLFAGTIYE NIAYGKKNAR ESEIRKAAML ANAHEFISGM NDGYAMYCGE
     RGVQLSGGQK QRIALARAIL KDPAILLLDE ATSALDSVSE SLVQEALEKM MVGRTCIVVA
     HRLSTIQKSN SIAVIKDGNV VEQGSHSDLL AIGRRSAYYS LVKPQGSNSP YR
//
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