ACRT_ASPA1
ID ACRT_ASPA1 Reviewed; 554 AA.
AC A0A1L9WQV4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Acurin A biosynthesis cluster MFS-type transporter {ECO:0000303|PubMed:32234543};
GN ORFNames=ASPACDRAFT_1881869;
OS Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=690307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 16872 / CBS 172.66 / WB 5094;
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=32234543; DOI=10.1016/j.fgb.2020.103378;
RA Wolff P.B., Nielsen M.L., Slot J.C., Andersen L.N., Petersen L.M.,
RA Isbrandt T., Holm D.K., Mortensen U.H., Noedvig C.S., Larsen T.O.,
RA Hoof J.B.;
RT "Acurin A, a novel hybrid compound, biosynthesized by individually
RT translated PKS- and NRPS-encoding genes in Aspergillus aculeatus.";
RL Fungal Genet. Biol. 139:103378-103378(2020).
CC -!- FUNCTION: MFS-type transporter that may have a role in the biosynthesis
CC of acurin A, a highly reduced polyketide coupled to a serine via a
CC peptide bond; either in extra- or intracellular transport.
CC {ECO:0000305|PubMed:32234543}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the acurin A cluster-
CC specific transcription regulator acrR. {ECO:0000269|PubMed:32234543}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the production of acurin A.
CC {ECO:0000269|PubMed:32234543}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV878980; OJJ98488.1; -; Genomic_DNA.
DR RefSeq; XP_020054828.1; XM_020198265.1.
DR AlphaFoldDB; A0A1L9WQV4; -.
DR SMR; A0A1L9WQV4; -.
DR EnsemblFungi; OJJ98488; OJJ98488; ASPACDRAFT_1881869.
DR GeneID; 30972079; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_1881869; -.
DR OrthoDB; 672661at2759; -.
DR Proteomes; UP000184546; 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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..554
FT /note="Acurin A biosynthesis cluster MFS-type transporter"
FT /id="PRO_0000450428"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 554 AA; 60268 MW; EA42DEF50239E510 CRC64;
MADHGEHGVP EQQNAPPKKG LRFWLIFLAI GIATFVAALD TSIISTALPT ITADLGSEEL
YIWIINTYLL SSTVSSAIVG QLSNIFGRRS MTTLALLIFA VGSAISGAAR DTGMLLAGRT
IQGLGGGSIT TLSEVLVCDM VSLRERGVYA GILGAAWTLA AVVGPIMGGG FTQNVSWRWI
FYINLPIAGS SLFLIVTLLR VRNPRSDTSI LRRLRTIDWG GITLLTLGVT AILLSLTWAG
TTHPWSSWRT IVPLILGFLG LLGFIAYEAL PPEPTMPLRL FRNRTAATLF VMAFIYSLLL
FWVCYFLPIY FQAVLNATPT RSAVMLFPVA TTTAPAGIVA GILMTKTGRY RSFQYIGFAL
MTIACGLFTL LDQSTTTGEW TGYQILFGVG TGIVFTTGLP PILASLPESD VATGTATWIF
MRNFGAIWGT AIPAAVFNTK ANALASQTID DPTVRGLLVN GGAYERATKA FVSSFKSRPA
VMRAIRRLYV VSLREVWQVS IAFCGVGFLL CFLVKAYRLR EELNTEYGMQ LWRPVFKRLV
CTWYLAGSAN LMCT
