NSRN_ASPN1
ID NSRN_ASPN1 Reviewed; 506 AA.
AC A0A2I1C3U4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=MFS-type transporter nsrN {ECO:0000303|PubMed:30394754};
DE AltName: Full=Neosartorin biosynthesis cluster protein N {ECO:0000303|PubMed:30394754};
GN Name=nsrN {ECO:0000303|PubMed:30394754}; ORFNames=P174DRAFT_373375;
OS Aspergillus novofumigatus (strain IBT 16806).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1392255;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 16806;
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kjaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
RN [2]
RP FUNCTION.
RX PubMed=30394754; DOI=10.1021/acs.orglett.8b03123;
RA Matsuda Y., Gotfredsen C.H., Larsen T.O.;
RT "Genetic characterization of neosartorin biosynthesis provides insight into
RT heterodimeric natural product generation.";
RL Org. Lett. 20:7197-7200(2018).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of the tetrahydroxanthone dimer neosartorin, which
CC exhibits antibacterial activity. {ECO:0000269|PubMed:30394754}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; 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; MSZS01000005; PKX92296.1; -; Genomic_DNA.
DR SMR; A0A2I1C3U4; -.
DR VEuPathDB; FungiDB:P174DRAFT_373375; -.
DR OrthoDB; 627633at2759; -.
DR Proteomes; UP000234474; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..506
FT /note="MFS-type transporter nsrN"
FT /id="PRO_0000453501"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 481..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 506 AA; 53459 MW; 6C5E5332F84C169E CRC64;
MFLVALDRTI LATAIPRITD EFHSLTSVGW YGSAYLLTCC ALQLIFGKIY TLFSVKWTLL
WSILIFEASS ALSGAAPNST ALIVGRAICG VGAAGIFAGV VVCIVHVVPL HKRPQIQGMF
GALMGVSSIV GPLIGGGFTS NVTWRWCFYI NLPVGGVAML VILVFLKIPD QPTAQAPLSE
KIKQLDIPGT VLLVPGTVCL LLALQWGGQT YPWSNGRVIA LLTLAGVLLV GFSAVQVLLP
RTATLPPRIM KQRSVAAACW ATLTINCGNY IIIYFLPIWF QSIKGASASE SGIRTLPLMI
SMVAGSISGG TLNTKIGYYT PLAIVGTCLM CVGNGLLTTF EVDTGAGKWI GYQILYGLGL
GLAFQVPNLA TQASLPKKDV PTGLALMLFA TLLGASVFVS AGENVLANQL VKRLAGVEGV
DISLITSGGA TSLLQSLPDG VRKIALVAYN EALREVFRVG LIPTCLSVLG AAALEWRSVK
KPAGKVSAED GEKETKNVDK ETTEKT