ID A6R5E3_AJECN Unreviewed; 833 AA.
AC A6R5E3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE SubName: Full=Sulfate permease II {ECO:0000313|EMBL:EDN08341.1};
GN ORFNames=HCAG_04851 {ECO:0000313|EMBL:EDN08341.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN08341.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476658; EDN08341.1; -; Genomic_DNA.
DR AlphaFoldDB; A6R5E3; -.
DR STRING; 339724.A6R5E3; -.
DR VEuPathDB; FungiDB:HCAG_04851; -.
DR HOGENOM; CLU_003182_8_1_1; -.
DR OMA; IFLPINH; -.
DR OrthoDB; 1082533at2759; -.
DR Proteomes; UP000009297; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000009297};
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 92..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 121..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 195..218
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 284..307
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 407..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 464..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 570..695
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 757..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 91306 MW; F2EBC641F548E5E0 CRC64;
MTNSKGGTST KVGNSLVKLA GIKKNYRDPI GEDPVTRGES TFSVGTSDTY AYVEQEPSSA
DWLRELVPTG QQVVQYFTNL FPFLRWITRY NLQWLIGITV GAVVVPQSMA YAKLAELKPQ
FGLYSSFMGV LIYWFFATSK DITIGPVAVM STLVGQVVIK VQANNPEIPA HYVASALAII
CGGIITFIGL IRCGWIVDFI PLTAITAFMT GSAISIAAGQ VPSMMGIRGF DTRDATFRVI
INTLKHLPDT KIDAAMGLTA LFLLYLIRWA CNFSARKNPN KQKLFFFLAT LRTAFVILLY
VMISWLVNKN HREKPIFRIL GTVPRVNTKI IKNFASDIPA AVIVLLIEHI AISKSFGRIN
NYTIDPSQEL VAIGVTNLLG PFLGGYPATG SFSRTAIKSK AGVRTPFAGV ITAVVVLLAI
YALPAVFFYI PNSSLSAVII HAVGDLITPP NTIYQFWRVS PLEVVIFFAG VLVTIFSSIE
NGIYCTVCVS AAILLFRVVK AQGQFLGRVK IHSVIGDHVQ GNDGKHGGAF EANSFNPSRA
NNPSSARNIF LPLNHNDGSN PEIEVEQPSP GIFIYQFSEG FNYPNANHYL DYLVSTIYKH
TRRTNLDSYP RLGDRPWCDP GPRKGQVEED RSHLPTLKAI ILDFSSVNNV DVTSIQNLID
VRNQLDRYAA PQPVHWHFAH INNRWTKRAL VSAGFGYPTP SPGGNGRWKA IFSVAELGGS
NSAAAHEALK RRRESDQYSD KFKQDVEAAT QAIGHISHKA GGEDGVEETS STESGNELGK
ELDSSKVYSV ASRRIVAVHG LNRPLFHMDL TSALQGALAN SEATAAENNI IRN
//