PGMG_ASPTN
ID PGMG_ASPTN Reviewed; 577 AA.
AC Q0CJC4;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=MFS-type transporter pgmG {ECO:0000303|PubMed:35351612};
DE AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein G {ECO:0000303|PubMed:35351612};
GN Name=pgmG {ECO:0000303|PubMed:28471414}; ORFNames=ATEG_06210;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RC STRAIN=MUCL38669;
RX PubMed=28471414; DOI=10.3390/microorganisms5020022;
RA Palonen E.K., Raina S., Brandt A., Meriluoto J., Keshavarz T., Soini J.T.;
RT "Melanisation of Aspergillus terreus-is butyrolactone I involved in the
RT regulation of both DOPA and DHN types of pigments in submerged culture?";
RL Microorganisms 5:0-0(2017).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=35351612; DOI=10.1016/j.fgb.2022.103690;
RA Tang S., Men P., Zhang W., Li H., Li Z., Huang X., Lu X.;
RT "Identification of a polyketide biosynthesis gene cluster by
RT transcriptional regulator activation in Aspergillus terreus.";
RL Fungal Genet. Biol. 160:103690-103690(2022).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of pleosporalin A, ascomycone A, as well as a third
CC cryptic naphthoquinone derived pigment, all responsible for the
CC coloration of conidia (PubMed:28471414, PubMed:35351612). Seems not to
CC be involved in pigment biosynthesis although its expression is
CC regulated by the cluster-specific transcription factor pgmR
CC (PubMed:35351612). {ECO:0000269|PubMed:28471414,
CC ECO:0000269|PubMed:35351612}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the pgm cluster-
CC specific transcription factor pgmR. {ECO:0000269|PubMed:35351612}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of the
CC naphthoquinones derived pigments. {ECO:0000269|PubMed:35351612}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC family. {ECO:0000305}.
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DR EMBL; CH476601; EAU33971.1; -; Genomic_DNA.
DR RefSeq; XP_001215388.1; XM_001215388.1.
DR STRING; 33178.CADATEAP00002979; -.
DR EnsemblFungi; EAU33971; EAU33971; ATEG_06210.
DR GeneID; 4321479; -.
DR VEuPathDB; FungiDB:ATEG_06210; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_000960_22_1_1; -.
DR OMA; ATYNAKW; -.
DR OrthoDB; 503593at2759; -.
DR Proteomes; UP000007963; 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; 2.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..577
FT /note="MFS-type transporter pgmG"
FT /id="PRO_0000456012"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
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 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 577 AA; 62204 MW; 7AF9F76BDE5A4DCF CRC64;
MSETVTQTET DQRPATARSL GAEEKEAKSD EQFQQERTIK GFRWFIVIIS ILSSVTLYSL
DNTIVADIQP QIINTFDELD KLPWLSVAFL VACVATNSIW SKIYSQLNAK WLYLFCVVLF
EVGSAMCGAA PTINTLIGGR ALAGLGGAGL YVGVMTLLSV NTSKRERPMY IGMTGLTWGV
GTVLGPIVGG GFAVSKVGWR WSFYINRECR PSVQPIRPLT VPPVFFAAVA IPIYLFMLPS
FDPRPGVSYK ERLAQLDYLG TILMIGACVS GVMAINFGGQ IYPWDSGQTI SCFVVSGVLF
IVFGLQQWYC IGTTKENRTF PCQFLARPAF IILFVQTASV ATVFFVPIYF VPLFFQFTRN
DSAIDAGVRL LPLVCFIVAA MILNGALMSK FGYYMPWYLV GGCLSLVGSV LMYTIKLGTS
TANIYGYMII LGVGGGMYAQ ASFAVAQGKA RPREIPVATG FISLAQLTGG TIALAIANSV
FLEKASAGIM AVVPDASKET VQSAISGASS SFFQTLDPDV REAVLAAVTH AISQVYILPI
TGAAMSISLA IFMPREKLFV ASDSGDRDGV TPLGAMG