AGN12_PAEDI
ID AGN12_PAEDI Reviewed; 433 AA.
AC A0A411PQP0;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Agnestins efflux protein AgnL12 {ECO:0000303|PubMed:30746079};
DE AltName: Full=Agnestins biosynthesis cluster protein L12 {ECO:0000303|PubMed:30746079};
GN Name=AgnL12 {ECO:0000303|PubMed:30746079};
OS Paecilomyces divaricatus (Penicillium divaricatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=644132;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K5013;
RX PubMed=30746079; DOI=10.1039/c8sc03778g;
RA Szwalbe A.J., Williams K., Song Z., de Mattos-Shipley K., Vincent J.L.,
RA Bailey A.M., Willis C.L., Cox R.J., Simpson T.J.;
RT "Characterisation of the biosynthetic pathway to agnestins A and B reveals
RT the reductive route to chrysophanol in fungi.";
RL Chem. Sci. 10:233-238(2019).
CC -!- FUNCTION: Efflux pump that may be involved in the secretion of
CC agnestins, dihydroxy-xanthone metabolites.
CC {ECO:0000269|PubMed:30746079}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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DR EMBL; MH898872; QBG38876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411PQP0; -.
DR SMR; A0A411PQP0; -.
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; -; 2.
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; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..433
FT /note="Agnestins efflux protein AgnL12"
FT /id="PRO_0000449024"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 46581 MW; 8158BD368EDCEC0C CRC64;
MSRSTSTELQ QELPASKEVP PDPTSIASSE TASGSKPPST EFTPRAILVL VGSFLVTFCS
VGFTNAFGVF QTYYQEAFLS DKSSSDISWI GSFNIFCMFG CTFISGYLTD RYGPRLLICF
GSLVMVFALF MLSLSTEYYQ IFLTQAFLFG VGISFVLLPA MATVSLYFAK SRSLAMGIIV
SGSSLGGVIW PIALDRLFNE VSFGWTVRIA AFIMLPLLGL ACLAIRRPAE FANRPKPKAD
FSCVKNPVMI FLAIGLFLIF LGLFSPFFYV TSYMISLGKD SNLAFYMVSV VNASSLFGRI
LPGLIADRVG NYNVLFMVAV FSGLVACCWT KATSVGGIVV FSLAYGLASG AVISLQGPCA
AQTVQREQFG VAMGVVMTFL SIAGLVGTPI NGQILIPYGY LGLSLFSGLV MLLGSVFILL
ARLKIKTGLL VKA