LNBF_ASPFN
ID LNBF_ASPFN Reviewed; 479 AA.
AC B8NWW7;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=MFS-type transporter lnaF {ECO:0000303|PubMed:23281040};
DE AltName: Full=Lnb diastereomeric piperazines biosynthesis cluster protein F {ECO:0000303|PubMed:23281040};
GN Name=lnaF {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_121540;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP IDENTIFICATION, FUNCTION, AND PATHWAY.
RX PubMed=23281040; DOI=10.1002/anie.201207456;
RA Forseth R.R., Amaike S., Schwenk D., Affeldt K.J., Hoffmeister D.,
RA Schroeder F.C., Keller N.P.;
RT "Homologous NRPS-like gene clusters mediate redundant small-molecule
RT biosynthesis in Aspergillus flavus.";
RL Angew. Chem. Int. Ed. 52:1590-1594(2013).
CC -!- FUNCTION: MFS-type transporter; part of the lnb gene cluster that
CC mediates the biosynthesis of diastereomeric piperazines. Lna and lnb
CC clusters encode sets of enzymes that produce overlapping sets of
CC previously undescribed metabolites such as piperazinomycin-like
CC metabolites or morpholine (PubMed:23281040). The lna and lnb
CC biosynthetic pathways appear to be part of a signaling network that
CC controls the formation of sclerotia, a resilient overwintering
CC structure (PubMed:23281040). May be involved in the secretion of the
CC metabolites produced by the lna and lnb clusters (Probable).
CC {ECO:0000269|PubMed:23281040, ECO:0000305|PubMed:23281040}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; EQ963485; EED45925.1; -; Genomic_DNA.
DR RefSeq; XP_002384861.1; XM_002384820.1.
DR AlphaFoldDB; B8NWW7; -.
DR SMR; B8NWW7; -.
DR STRING; 5059.CADAFLAP00012726; -.
DR EnsemblFungi; EED45925; EED45925; AFLA_121540.
DR VEuPathDB; FungiDB:AFLA_121540; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_1_1; -.
DR OMA; TSSHATW; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..479
FT /note="MFS-type transporter lnaF"
FT /id="PRO_0000446084"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 479 AA; 51372 MW; 4324FEA2F2543D4C CRC64;
MATAIPKITD QFHSAQDIGW YGSSYLLTNS CLTISFGKLY TLYPVKWIYL VALALFEIGS
LVCGFTPNSV GLIIGRAITG LGSAGLFSGA ITVISQSMPL QRRLLCISVI MCLFGVADVA
GPLIGGVFTD YLTWRWCFYI NLPFGGLTAL AIVFLLEAQQ PVKQAGGIKC LLSHLDLVGL
LFLFPAVICL LLVLSWGGAD YPWDDRRIIG LIVGFTALIL VFIVVQWWKQ DKATVPPRLI
KKRDIWGTSI FSFCITGAMM AFTYHLPIWF QSVKGVSATK SGLMSIPTIL GMTICSLLSA
VLVGKIGFYT PFMYAAPVLS VIGAGLLSTL KVDSGPAQWI GYQIPFGIGL GIGLSQPMVV
VQAVLEPDDI PLAIAITAFM ESLGGSVAIS VAQSVFRSQL VKNMALEAPQ ANAHGNITTA
MTTLRDTVPP EMLSGVLRAY NLAITQALYV GVALSSLAIV GALPIRWTSV NEKKTEGCP
