ID U1HH53_ENDPU Unreviewed; 1341 AA.
AC U1HH53;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Major facilitator superfamily (MFS) profile domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EPUS_01829 {ECO:0000313|EMBL:ERF69500.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF69500.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000256|ARBA:ARBA00010992}.
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DR EMBL; KE721402; ERF69500.1; -; Genomic_DNA.
DR RefSeq; XP_007804757.1; XM_007806566.1.
DR GeneID; 19236884; -.
DR eggNOG; KOG0254; Eukaryota.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_258351_0_0_1; -.
DR OrthoDB; 1348131at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR CDD; cd09630; CDH_like_cytochrome; 1.
DR CDD; cd08760; Cyt_b561_FRRS1_like; 1.
DR Gene3D; 1.20.120.1770; -; 1.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 2.
DR Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR015920; Cellobiose_DH_cyt.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003099; Prephen_DH.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR NCBIfam; TIGR00879; SP; 1.
DR PANTHER; PTHR48022; PLASTIDIC GLUCOSE TRANSPORTER 4; 1.
DR PANTHER; PTHR48022:SF26; SUGAR TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G11050)-RELATED; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SMART; SM00665; B561; 1.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
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 TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 704..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 950..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 981..1002
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1115..1132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1144..1162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1183..1204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1236..1255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..274
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 780..1274
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 588..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1341 AA; 147258 MW; E5769B9EDC9C0D19 CRC64;
MDHISVGIIG MGDMGKIVNA CDTPDKYDDL LAQFAGQDMV TVMPNGHLVS RSSDWIIYSV
PAEGIGKIVA EFGPSTKLGA IVGGQTSCKA PEIAAFESYL PKDVEIISCH SLHGPQVHPK
SQPLVIIPHR ASEKSVKLVE SILSSFESKI VHLSGDKHDR ITADTQAVTH VAFLSMGSAW
RANNQFPWEI NRYVGGIENV KINITLRIYS NKWHVYAGLA ILNPSAQQQI RQYAKSVTEL
FKLMIGGHRK ELENRVKTAG ATIFGDVVKG HELLLRDDIL DKFSLSGPKE RMPNNHLSLL
GIVDCWWKLN INPYDHMICS TPLFRIWLGV TEYLFRSEQL LDEVINTAIE DDTFRSDDLE
FTFAARAWSD CVSFGNFDSY RERFEEIQKH FEPRFADAVR LVVGIVNGQV QVATYVPQGS
DANGVSYSVN IPSSTAQSGN GPIYIQMVAP SGTQWLGLGQ GSGMAGANMF VMYSSGSNNV
TLSPRLGRGE FPPEVNPAGE ITLLEGTGVS AEGVMTANIR CDSCITWDGG SMSPTNGNSN
WIWAIRQGNA LDSGDISAQI RQHDAYGAFT FDLPAGTSSD SSNPFVQAAA VTQSAGSSEP
SSPGDSEASS GESSSRSSGS SSGSSSGGQS NTDQIRMSHG TIMAVVFLFL FPIGALMIYL
PVSRRVPYIH APIQVVSTCL LIVGMILGVI LGVRIDEDDG YHQIIGYIVV SSLLLFQPAL
GLIQHLRYRK LGKRTVFGHI HRWLGRILIL LGIINGGLGL HISGEIGSEQ VPRWSVIAYS
VVAAVVGIVY LALASGVGFS RKRKGGSKEE TELNGNASGD MDTNAYHPES FGYDQGVFGG
VIVTDDFLNT LGLNGPQHVS TVSTVTAIYD VGCFLGACFS IWYGEKFGRR FTVLTGTTIM
SIGAVLQIAA YGVPQMIIGR IVGGIGNGMN TATAPVWQSE TSQIKWRGKL VVLEMILNIA
GFSISNWVTY GFSFLGGPIS WRFPLAFQFV FIFILFATTP WLPESPRWLI AHEREDEAFE
ILADLEGKDP NDPFILTQHK EIVYAVQYEK KNAIPWSKLL MGKTGSGGGT KTMRRIILGA
GTQAMQQLSG INVTSYYLPT VLIESVGLEN SQARLLAACN SISYLLFSFI GIPNVERWGR
RKMMMYAAAG QCFCYLMITV LLRHTEIPSY PEEKQAKIAS ASIAFFFLYY VFFGIGWQGV
PWLYPTEINS LSMRTKGAAI VVEITPPGIQ SLQWKFYMIW TVFNGAFVPI VYLFYPETAD
RSLEDIDRMY RENPKLLVFR DKSITSSKRP MEYIQHEEEQ LRRNGSVDPA MLRRGSKITS
PIPNNEDTDY IEHNVVAEDK V
//
