LNAF_ASPFN
ID LNAF_ASPFN Reviewed; 494 AA.
AC B8NU03;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=MFS-type transporter lnaF {ECO:0000303|PubMed:23281040};
DE AltName: Full=Lna diastereomeric piperazines biosynthesis cluster protein F {ECO:0000303|PubMed:23281040};
GN Name=lnaF {ECO:0000303|PubMed:23281040}; ORFNames=AFLA_101740;
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, INDUCTION, 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 lna 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. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; EQ963484; EED46510.1; -; Genomic_DNA.
DR RefSeq; XP_002384046.1; XM_002384005.1.
DR AlphaFoldDB; B8NU03; -.
DR SMR; B8NU03; -.
DR STRING; 5059.CADAFLAP00011911; -.
DR EnsemblFungi; EED46510; EED46510; AFLA_101740.
DR VEuPathDB; FungiDB:AFLA_101740; -.
DR eggNOG; KOG0252; Eukaryota.
DR HOGENOM; CLU_001265_46_12_1; -.
DR OMA; CFTPLQD; -.
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; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF00083; Sugar_tr; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..494
FT /note="MFS-type transporter lnaF"
FT /id="PRO_0000446083"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 494 AA; 54332 MW; DF3E4F618466FA99 CRC64;
MTYDPENAMG EARADAPVEA EKEHEATQTT VKESTLGYDN SSDPSRRDSY RPTKLQSNLT
IVSCYIANFS DGFQNSLANP TNVIFKKLLG TDGYPSEMQT RISNSLLIGA ILGVLALGYT
SDMFSRRAGL LFTSGLVAIG TLMSTLALQV HPTYNMLWYF VIVRGIAGFG VGGEYPPSAA
AGIEESDDFK RKYRGPLFVS FTTLMATSAA PIQMIVYLIC LIASNDNLPV TFHAIYSIAT
ILPVIIMVLR FFMTDSTLFH YSNFKRQKRP LKFYLLLLKR YRWRLFTTSL AFFLYDFINF
PNSIMSSTII NSLVKDHNIR TTAIWQVILG ALPVPGVIVG AWLTNAIGRR YTGILGFAGY
MVLGFVIGGT FPHLSKNMPA FVVLYGLLQA LGHMGPGATI GLISTESFPT AMRGMGYSIA
TAFGRTGAAV GTQCFTPLQE RAGKQSTFYL AGGIAILGMI VYWFLPESSE LNLEEEDRDL
SVFLAENGFP MEKA
