ID A0A1Q9PC78_9ARCH Unreviewed; 473 AA.
AC A0A1Q9PC78;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Major facilitator superfamily (MFS) profile domain-containing protein {ECO:0000259|PROSITE:PS50850};
GN ORFNames=HeimAB125_14170 {ECO:0000313|EMBL:OLS31913.1};
OS Candidatus Heimdallarchaeota archaeon AB_125.
OC Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX NCBI_TaxID=1841596 {ECO:0000313|EMBL:OLS31913.1, ECO:0000313|Proteomes:UP000186239};
RN [1] {ECO:0000313|EMBL:OLS31913.1, ECO:0000313|Proteomes:UP000186239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB_125 {ECO:0000313|EMBL:OLS31913.1};
RX PubMed=28077874; DOI=10.1038/nature21031;
RA Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA Baker B.J., Spang A., Ettema T.J.G.;
RT "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL Nature 541:353-358(2017).
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:OLS31913.1}.
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DR EMBL; MEHH01000091; OLS31913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9PC78; -.
DR Proteomes; UP000186239; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR039672; MFS_2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11328:SF24; INNER MEMBRANE SYMPORTER YICJ-RELATED; 1.
DR PANTHER; PTHR11328; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13347; MFS_2; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 251..473
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
SQ SEQUENCE 473 AA; 53754 MW; 838547A8EFD542EB CRC64;
MTMKNPFKSL SDNLEVPFKF NLAYATGEIT DAVAYQGFSF LIFVYYFAVI GIEFKYMVIV
YALWSVYNAF NDPIIGGLCD KTKTKRFGGG RRRPWMVAMW LPLAAVMFFL FTPFTTFAQH
PVWVVIYFFV VICLFDTVYT GFSLSRTSLY PEMFRTNKAR EEAGAGRRIM MIFGLILAMG
VPTLFIPKLT EPGQENIYNY WIAGAVLGAI VLVTAFINIK WGVKEPPLEE LEKKETLGVF
KAIWYCMKNW KFMIFIFCSM MNWYIFAIFP MMMPFFSEFV LGESNSMLVV LLLLIAFLSS
AIGVLIWSFV DSKIGSKYGF VLSQLYWIAV LIPLFFVENY WVAFVLMALN GIGLGGSPYF
IDRNISNIAD EDELKTGKRR EGAYYGVHAL VIRFSGIFSI VSAYIVLGPY GWNAFSPAVV
NVQILTGLKL LVSFLPAGAL VIGIILLLLY PLDKKKVDEM QSAYKKEIKQ QES
//
