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Database: UniProt
Entry: A0A1L9R9R8_ASPWE
LinkDB: A0A1L9R9R8_ASPWE
Original site: A0A1L9R9R8_ASPWE 
ID   A0A1L9R9R8_ASPWE        Unreviewed;       775 AA.
AC   A0A1L9R9R8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=STAS domain-containing protein {ECO:0000259|PROSITE:PS50801};
GN   ORFNames=ASPWEDRAFT_163873 {ECO:0000313|EMBL:OJJ31662.1};
OS   Aspergillus wentii DTO 134E9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Cremei.
OX   NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ31662.1, ECO:0000313|Proteomes:UP000184383};
RN   [1] {ECO:0000313|Proteomes:UP000184383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU362052}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362052}.
CC   -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.
CC       {ECO:0000256|ARBA:ARBA00008692, ECO:0000256|RuleBase:RU362052}.
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DR   EMBL; KV878216; OJJ31662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9R9R8; -.
DR   STRING; 1073089.A0A1L9R9R8; -.
DR   VEuPathDB; FungiDB:ASPWEDRAFT_163873; -.
DR   OrthoDB; 1082533at2759; -.
DR   Proteomes; UP000184383; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   InterPro; IPR018045; S04_transporter_CS.
DR   InterPro; IPR011547; SLC26A/SulP_dom.
DR   InterPro; IPR001902; SLC26A/SulP_fam.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   NCBIfam; TIGR00815; sulP; 1.
DR   PANTHER; PTHR11814:SF55; SODIUM-INDEPENDENT SULFATE ANION TRANSPORTER; 1.
DR   PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SUPFAM; SSF52091; SpoIIaa-like; 1.
DR   PROSITE; PS01130; SLC26A; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184383};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362052};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362052}; Transport {ECO:0000256|RuleBase:RU362052}.
FT   TRANSMEM        70..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        100..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        125..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        156..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        269..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        323..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        400..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        457..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   DOMAIN          556..683
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   REGION          595..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  85556 MW;  219F0EB0A822CDA6 CRC64;
     MSKVGHGVAK VLGVKLADSV PYDNMPSYAY IEPEPTLADW FREHTPTSSQ VGRYFYDLFP
     FLHWILCYNW QWFVGDLIAG VTVGAVVIPQ GMAYANLAQL PAEYGLYSSF MGVLIYWFFA
     TSKDITIGPV AVMSTLVGTI IIETQAKHPE LDAPTIASAL AIICGAITFF LGLIRFGFIV
     DFIPLPAITA FMTGSAINVC AGQVKSMLGE TAGFSTRGAT YKVIINTLKY LPTSQMDAAM
     GLTALAMLYS IRSACTFGSK RMSHKAKTFF FISTLRTVFV ILFYTMISAA VNLHRRDDPA
     FKLLGNVPRG FKHAHVPKVN TEIISSFASE LPAAVIVLVI EHIAISKCFG RVNNYTIDPS
     QEFVAIGVSN LLGPFLGGYP CTGSFSRTAI KAKAGVRTPL AGVITAVVVL LAIYALPALF
     FYIPKSSLSA VIIHAVGDLI TPPSTAYHFW RVSPLDAIIF IAGVIITVFT SIEIGIYCTI
     CVSIAILLFR IAKAQGQFLG QVKIQTIIGD YMNDEQKYRL QDIQFNQDEQ SYRSIFLPVK
     HTDGSNPNIK MDQPSPGIFV YRLSDGFNYP NANHYTDHLV ETIYQSTRRT NAFSYGSLGD
     RPWNDPGPRQ RKGEVEDVSS KLPTLRAIIL DFSSVNNVDV TCIQNLIDVR NQLDRHAHPE
     PVDWHFAHVN NRWTKRALVA AGFGFPSPRP DGQQWKSIFS VAEIAGSTIP DTADEARFND
     VEGGYKKYPQ TSEHERNESD ASINRDRMTM VNGINRPLFH PDLASALHIA TANRK
//
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