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Database: UniProt
Entry: A0A2G5HJQ0_CERBT
LinkDB: A0A2G5HJQ0_CERBT
Original site: A0A2G5HJQ0_CERBT 
ID   A0A2G5HJQ0_CERBT        Unreviewed;       822 AA.
AC   A0A2G5HJQ0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Sulfate permease 2 {ECO:0000313|EMBL:PIA92759.1};
GN   ORFNames=CB0940_04169 {ECO:0000313|EMBL:PIA92759.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA92759.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA92759.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA92759.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIA92759.1}.
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DR   EMBL; LKMD01000105; PIA92759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HJQ0; -.
DR   OrthoDB; 1082533at2759; -.
DR   Proteomes; UP000230605; Chromosome 4.
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   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        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        118..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        141..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        192..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        253..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        284..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        342..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        419..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   TRANSMEM        478..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362052"
FT   DOMAIN          581..706
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
FT   REGION          615..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..766
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   822 AA;  89155 MW;  73B8876FCD611C84 CRC64;
     MASTSTKIGH GLAKVLGIKL DDGTPGSKLS RGESVFSVES ADSYVEQEPT AAEWLRDVIP
     SGTDVLHYCH NLFPFTKWIL RYNAQWLYGD LVAGITVGAV VVPQSMAYAQ LAQLPVEYGL
     YSSFMGVLIY WFFATSKDIT IGPVAVMSTI VGNIVISVAK KDPTIEGHVV ASALAVIVGA
     IVCFLGLARL GWLVEFISLA SISAFMTGSA INIAVGQVPA LMGISSKIVN NRDSTYLVVI
     NTLKHLGSSK LDAALGLTAL TMLYLIRSSL NFAARKQPQH KKLYFFLATL RTAFVILLYT
     MIAWLMNLNL EDHDAKKSPI AILGTVPRGF KHAAVPTVNS NIISLFAGEL PASVIVLLIE
     HISISKSFGR VNNYTIDPSQ ELVAIGVTNL LGPFLGGYPA TGSFSRTAIK SKAGVRTPFA
     GVITAVVVLL SIYALPAVFF YIPKAALSAV IIHAVGDLIT PPNTVYQFWR VSPLEVPIFF
     AGVIITVFTT IEIGVYVTVA ASAALLIFRL FKAQGRFLGK VKVRDMPSGQ LIDGEAKRSG
     SGAGTGAVAN GHDSYPTRDV FIPFDNQDGS NPAIQPQHAY PGVFIFRFSE GFNYPNANHY
     LDYLSKVIFE QTQRTNPHSY ARPGDRPWND PGPRPGKEVN VDDHRPTLKA IVIDFSSVNN
     VDLTSIQNLI DVRNQLDRYT APERVQWHFA CINNRWTKRA LANAGFGYPS VDSEDAFQRW
     KPIFSVAEIG GASSAAAAGD EAYSKQFYHT QSKDLESRRP DDDSINASES SSDINTQLKD
     SATYKAKVAV VQGLNRPFFH IDVTSAVQSA VSGIEAQGKN VE
//
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