ID   NTT1_PARGY              Reviewed;         548 AA.
AC   Q4LCA6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=ADP,ATP carrier protein 1;
DE   AltName: Full=ADP/ATP translocase 1;
DE   AltName: Full=Nucleotide transporter 1;
GN   Name=ANC1;
OS   Paranosema grylli (Microsporidian parasite) (Nosema grylli).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC   Paranosema.
OX   NCBI_TaxID=235222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Dolgikh V.V., Trezeguet V., David C., Lauquin G.J.-M.;
RT   "The occurrence of protein similar to bacterial-plastidic ATP/ADP
RT   translocase is common for microsporidia: encoding genes are present in two
RT   distantly related species.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP transporter involved in the uptake of ATP from the host
CC       cell cytoplasm. Provides the microsporidian cell with host ATP in
CC       exchange for ADP. This is an obligate exchange system. This energy
CC       acquiring activity is an important component of microsporidian
CC       parasitism (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ADP/ATP translocase tlc family.
CC       {ECO:0000305}.
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DR   EMBL; AJ868111; CAI30461.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4LCA6; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR   InterPro; IPR004667; ADP_ATP_car_bac_type.
DR   PANTHER; PTHR31187; PTHR31187; 1.
DR   Pfam; PF03219; TLC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..548
FT                   /note="ADP,ATP carrier protein 1"
FT                   /id="PRO_0000382924"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   548 AA;  61503 MW;  9AF68D1DB26FF573 CRC64;
     MTKIENCKSC LPTENEVEEE ALSGVTFLGR VFKVARCERP VFTYMSIILF LVSYIYSVSR
     DMKDAIIIER LDPASIPYLK VLVVLPVNIC IVFSIQKILI NTSVSKVFSI MCVMFGIYFC
     LYGTVLMSFR HIFELNEFLI RDWFADDKMV FMGLQWTIAL ALPVNSWTSS LMYLSAEIWG
     TVVFQFLFFA LSNEIYTQKQ SLRFIPLFLV FGNVALIVSG FSMKFIKYVS EQGSYEFTLF
     FRKLVFVLMG ICSFVIYLIH RYFEDNIAHK PLFVTSEASY KQKTKSKIGF MEAMQTMASS
     RLVLAISFVV IAYSVSVNMV EASFKTCMSQ YALQKGAQAD FHVMGVQSDI QLAVGALSII
     LLLSSFPALI RDKGFLYVAF VPPIFCIFGM ASVFGMAALN NSARGNRTLL GFVSIGENLW
     LEQLLGAIIV TGFKILKYSA VDVSKEALSM RINPAYRARF KGIYDGVCGK LGKAIGSGIT
     NMQNVFYNSS DVRKAAISSL TIVTVITACW GFAVRYLAGK YDKSTHSNTD IDIDLINVDP
     MEKDADDL