PRHG_PENBI
ID PRHG_PENBI Reviewed; 589 AA.
AC A0A1E1FFK8;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=MFS-type transporter prhG {ECO:0000303|PubMed:27602587};
DE AltName: Full=Paraherquonin biosynthesis cluster protein G {ECO:0000303|PubMed:27602587};
GN Name=prhG {ECO:0000303|PubMed:27602587};
OS Penicillium brasilianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=104259;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 22354 / NBRC 6234 / CBS 338.59 / FRR 3454 / IMI 68220;
RX PubMed=27602587; DOI=10.1021/jacs.6b08424;
RA Matsuda Y., Iwabuchi T., Fujimoto T., Awakawa T., Nakashima Y., Mori T.,
RA Zhang H., Hayashi F., Abe I.;
RT "Discovery of key dioxygenases that diverged the paraherquonin and
RT acetoxydehydroaustin pathways in Penicillium brasilianum.";
RL J. Am. Chem. Soc. 138:12671-12677(2016).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of paraherquonin, a meroterpenoid with a unique,
CC highly congested hexacyclic molecular architecture.
CC {ECO:0000269|PubMed:27602587}.
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; LC127182; BAV69308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1FFK8; -.
DR SMR; A0A1E1FFK8; -.
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; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..589
FT /note="MFS-type transporter prhG"
FT /id="PRO_0000449172"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 589 AA; 62788 MW; C47485DDD5F35720 CRC64;
MITESREHLQ SKPQNSESII RLDTPDDRPS LECDSLPSGG HSSKVSGGPA SIEGKDVKNV
SELETCATKA QTPHDEVPIS TSKIIAVVGG LVLAVFCMSL DSTILSTAIP NIVSQFHSQN
EMGWYVSAYS LTLASFSLAF GKIYTFYSTK TVFLITLSLF EAGSLICGAA PNSLALIIGR
AIAGIGGTGM YLGALLLVAE ILPFDKIPIT TALLGAMYGI AAVVGPLLGG AFTDYATWRW
CFYINLPMGG LTFLFVFFFV KRGKDKKRTR EANNIVARFL ELDPIGVALM IPTLVCLLLA
LEWGGATYSW HSWRLIVLYV VGGCCALGFV GVQIWRQDTA TIPPRLLKNR NILGIILFSF
CLNGSFVVLA YYLPIWFQSI KGVTAIKSGI MNLPLILTMI ICSMICSTLV TKLGYYTPFL
YLAPIIASTG AGLLSTMHVN SGSPVWIGFQ ALFGIGLGCG GTLSIVAAQT ALPPEDISTG
TAIVTFTQTL AAAVFNFVAQ NVFQNQVLSG LAQSAPGVSA AKLTKAGPTM LREVVPADTL
PAVLEVYNTA ITRAFYVSVG GAALAIFGSI PLQWLSVKDR KTQAVTAHA