ID A0A1R3IDI6_COCAP Unreviewed; 833 AA.
AC A0A1R3IDI6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Biopterin transport-related protein BT1 {ECO:0000313|EMBL:OMO80620.1};
GN ORFNames=CCACVL1_12848 {ECO:0000313|EMBL:OMO80620.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO80620.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO80620.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO80620.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Folate-
CC biopterin transporter (TC 2.A.71) family.
CC {ECO:0000256|ARBA:ARBA00007015}.
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:OMO80620.1}.
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DR EMBL; AWWV01010286; OMO80620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3IDI6; -.
DR EnsemblPlants; OMO80620; OMO80620; CCACVL1_12848.
DR Gramene; OMO80620; OMO80620; CCACVL1_12848.
DR OrthoDB; 241511at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd17484; MFS_FBT; 1.
DR Gene3D; 6.10.140.180; -; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR039309; BT1.
DR InterPro; IPR004324; FBT.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00788; fbt; 1.
DR PANTHER; PTHR31585; FOLATE-BIOPTERIN TRANSPORTER 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31585:SF7; FOLATE-BIOPTERIN TRANSPORTER 4-RELATED; 1.
DR Pfam; PF03092; BT1; 1.
DR Pfam; PF04157; EAP30; 1.
DR Pfam; PF01190; Pollen_Ole_e_1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..833
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010181642"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 331..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 92618 MW; CBC37C82B7436E0C CRC64;
MESKNKNLVL SFVFLAVFLT PGVKSWTGEI HGRVVCDVCA DSSIGPEDHV LEGAEVAVLC
ITKSGEVVNY QAFTNAKGIY TVAETMPESD RWDACLARPI SSFHDRCNHL GEGSTGVKFT
YNRPSVTTYN IRKRGFRSFV WTAVSYQLKD MLKLSPSASQ FIFSIAFFPW SVKPIYGILS
DCIPIRGKKR IPYLIIASVM SLVPWLILGS NTTSRSSTWH LVILLTVQNL GSAMADVVVD
AMIAEAVRDE KASFAGDLQS VSWLAMAFGG VFGSLLGGYA LTNLEIAIVF LLFSILPAIQ
LFSCGLVEEN PINSGVLSEL SEFSNSHDLN GKANHLDEDS SLERKSSVNA RRRKKNQKKS
KRRQVMPSKA QNSRKGKSLL GQWFQSLKTA TYSLCRAFKQ PIILRPMAWF FLAHVTVPNL
STVMFYYQTE FLKLEASFLG TARVIGWLGL MVGTFTYNQY LKKMKLRRIL MFSHIGLAFL
IVFDIVLVSR TNVAFGISDK TMVLWGSALS DAINQLKFMP FLILSGQLCP PGIEGTLFAL
FMSINNFGST VGSFVGAGLA SILNISSGSF DNLLLGIVFE EKKMRRRPGI GGLQTAAAAR
DQYRLLGENV AKLRTDLMKE QLATFRSQLE EFARKHKNDI RKNPAFRSQF HEMCAKVGVD
PLASNKGFWA ELLGIGDFYY ELGVQIVEIC LSTRPLNGGL IDLQELCKLL RQKRKYDREA
VSEDDCLRAI SKLKTLGSGF EVISAGKKKL VRSVPTELKK DHNEILELAQ AQGYVTVDEV
ERRLSWTHGR AIDALDTLLE EGLAMIDDGH RDGKRRYWFP CVSSISSSFG ADS
//