ID A0A2V5HT89_9EURO Unreviewed; 836 AA.
AC A0A2V5HT89;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Sulfate permease {ECO:0000313|EMBL:PYI25902.1};
GN ORFNames=BP00DRAFT_80939 {ECO:0000313|EMBL:PYI25902.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI25902.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI25902.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI25902.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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; KZ825620; PYI25902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5HT89; -.
DR Proteomes; UP000248817; 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 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 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 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 121..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 259..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 289..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 421..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 478..510
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 581..707
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 620..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 91978 MW; 927C76D5697C77C4 CRC64;
MSKDFTTKVG HGLAKGLGIK QAYRDPLGAQ ADPVTRGEST FSYGTIDTYS YLEQEPTTAE
WFKEITPSWH DVGRYFYRLF PFLSWITRYN TQWLVGDLVA GITVGAVVVP QGMAYAKLAE
LPVQYGLYSS FMGVLLYWFF ATSKDITIGP VAVMSTLVGT IVLDAEDKYP NIPGHVVASC
LAIVSGGIVC ALGLLRLGFI VDFIPLPAIS AFMTGSALNI ASGQVKNLLG ESASFSTRDA
TYMIIINSLK HLPSAGIDAA LGVTSLAMLY MIRSACNFLA RKYPQKAKLW FFMSTLRTVF
VILFYTMISA AVNLHRKDDP MFNVIGNVPR GFKDAGVPRV DSEVISVFAS QLPACVIVLL
IEHIAISKSF GRVNNYTIDP SQELVAIGVT NLLGPFLGAY PATGSFSRTA IKSKAGVRTP
LAGVITAIVV LLAIYALTAV FFYIPQAALS GVIIHAVGDL ITPPNTVYQF WRVSPIDALI
FFIGVIVTVF SSIEDGIYCT ICVSVAVLLF RVAKARGQFL GRVTIHSVIG DHLVQGDGKY
GSGNNANSSD RDEEGSRRSI FLPLNHADGS NPEVGLEQPY PGIFIYRFSE GFNYPNANHY
TDYLVQTIFR ETRRTIPFSY EQRGDRPWND PGPRKNSAQE EQRSQRPLLR AVILDFSSVN
NVDVTSIQNL IDVRNQLDLY ASPRAVQWHF AHLNNRWTKR ALAAAGFGFP TPNSDNGFHR
WKPIFSVAEI EGRSSAAAHA ELLNNQHAQH VAQKRDEEDG LKHDGHTTER ETHGVEEGSD
ISSVPEDKLQ HDLNDSKAYR NRRKVAVVQG INRPFFHIDL TSALESALAN APPEDE
//