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Database: UniProt
Entry: A0A2P5F7Z7_TREOI
LinkDB: A0A2P5F7Z7_TREOI
Original site: A0A2P5F7Z7_TREOI 
ID   A0A2P5F7Z7_TREOI        Unreviewed;      1252 AA.
AC   A0A2P5F7Z7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=ABC transporter {ECO:0000313|EMBL:PON93923.1};
GN   Name=TorPGP14 {ECO:0000313|EMBL:PON93923.1};
GN   ORFNames=TorRG33x02_103130 {ECO:0000313|EMBL:PON93923.1};
OS   Trema orientale (Charcoal tree) (Celtis orientalis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Trema.
OX   NCBI_TaxID=63057 {ECO:0000313|EMBL:PON93923.1, ECO:0000313|Proteomes:UP000237000};
RN   [1] {ECO:0000313|Proteomes:UP000237000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) 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:PON93923.1}.
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DR   EMBL; JXTC01000055; PON93923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5F7Z7; -.
DR   STRING; 63057.A0A2P5F7Z7; -.
DR   InParanoid; A0A2P5F7Z7; -.
DR   OrthoDB; 5487044at2759; -.
DR   Proteomes; UP000237000; 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; ABC TRANSPORTER B FAMILY; 1.
DR   PANTHER; PTHR24222:SF62; ABC TRANSPORTER B FAMILY MEMBER 13-LIKE; 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:UP000237000};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        272..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        682..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        726..748
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        811..840
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        910..929
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        949..966
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..336
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          371..606
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          684..971
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          629..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1252 AA;  136299 MW;  767A81BDEF383A57 CRC64;
     MEEVELATNE VLEQNPVPKM DQPDRKTGTV SLFGLFSTAD KVDYVLMFFG SVGACVHGAA
     LPVFFVLFGR MIDSLGHLSK NSQRLSSRVS ENALYLIYLG VIVMVSAWIG VGFWMQTGER
     QTARLRVKYL ESILKKDISF FDTEARDANI IFHISSDTIL VQDAIGDKTG HALRYLSQFI
     VGFAIGFTSV WRLTLLTLAV VPLIAVAGVA YTLIMSTFSQ KSENAYAEAG KVAEEVISQV
     RTVYSFSGED RAVKAYSISL NKALKLGKKS GFAKGIGVGF TYGLLFCAWS LLLWYAGVLV
     RHGETNGGKA FTTIINVIFS GFALGQAAPN LAAIAKGQAA AANILSMIKT DLNSPNRSDN
     GIVLPKVSGQ IEFCDVRYAY PSRPDMVFEK LNFTVSSGKT SAVVGPSGSG KSTIISMVQR
     FYEPNSGKIL LDGHDLKTLQ LKWLREQMGL VSQEPALFAT TIVGNIMFGK DDVDMNQIIE
     AAKAANAHSF IEGLPDGYYT QVGEGGTQLS GGQKQRIAIA RAVLRNPKIL LLDEATSALD
     AESELIVQQA LDKIMSDRTT IVVAHRLSTI RDVDMIIVLK NGEVVENGTH SELISKKGEY
     ATLVSLQVSE QAEISSVFSV SQSSRNSSFR ELSKNQHHEE DLNSITGKEL GPSDHKEMSS
     SSFGPTPSIW ELVKLNTPEW PYAILGSVGA ILAGMEAPLF ALAITHVLTA FYSADDSRIK
     QEIQRVALIF VGLAVVTIPV YLLQHYFYTF MGERLTSRVR LLMFSAILSN EVGWFDLDEN
     NTGSLTSILA ADATLVRSAL ADRLSTIVQN IALTVTAFVI AFILCWRIAA VVIASLPLLI
     GASIADQLFL KGFGGDYNRA YSRATSVARE AVANIRTVAA FGAEDRLSAQ FASELNQPSR
     QAFLRGHISG FCYGVSQLFA FCSYALGLWY GSVLIRKNDS NFGDIMKSFM VLIITALAIA
     ETLALAPDIV KGSQALGSVF RVLQRKTLMN PNNPGSNIVT DIKGDIQFRN VSFRYPTRPN
     MAIFDDLNLE VLAGKSLAVV GPSGSGKSTV IGLVLRFYDP NLGAVLIDGY DIKSLNLRSL
     RKKIGLVQQE PALFATTIYD NIKYGKEEAS EIEVMKAARA ANAHGFITRM PEGYQTQVGD
     RGIQLSGGQK QRVAIARAIL KDPSILLLDE ATSALDASSE KLVQEALESL MERRTTIMVA
     HRLSTIRDAD NIAVLQNGKV VEVGSHEQLI AKSGGIYREL VSLQQEEYRN TA
//
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