ID A0A178BD75_9PLEO Unreviewed; 829 AA.
AC A0A178BD75;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Sulfate permease-like protein {ECO:0000313|EMBL:OAL07651.1};
GN ORFNames=IQ06DRAFT_372602 {ECO:0000313|EMBL:OAL07651.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL07651.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL07651.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL07651.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441705; OAL07651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178BD75; -.
DR STRING; 765868.A0A178BD75; -.
DR InParanoid; A0A178BD75; -.
DR OrthoDB; 1082533at2759; -.
DR Proteomes; UP000077206; 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:UP000077206};
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..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 141..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 171..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 198..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 242..264
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 284..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 440..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 470..487
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 578..703
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 613..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 91091 MW; D03122053410A583 CRC64;
MATTATKVGH GLAKVLGIDL HYRNETGSDR ITRGESVFSI DSADTYVERE PTTIEWLQDT
LPNGHDLGQY LYSLFPFVHW IGRYNLQWLI GDLVAGITVG AVVVPQGMAY ASLAQLPVEF
GLYSSFMGVL IYWFFATSKD ITIGPVAVLS TVTGSVILKA HEKVPDVPKD IIASSLAIIA
GSIVLFMGLA RLGWIVDVIS LPAISAFMTG SAISIAVGQV VDMMGVSGFN KREATYKVII
NILKHLGTTN LNASFGLTAL FLLYFIRWLC GFLARRHPSR QKLFFFLSTL RTAFVILLYV
LFSYLVNRHH RANKTKPKIS TIGNVPRGFQ HARVPHITPR IISSFASELP STVIVLLIEH
ISIAKSFGRV NNYVINPSQE LVAIGITNCL GPFLGAYPAT GSFSRTAIKS KAGVRTPFAG
VITAVVVLLA IYALPAMFWY IPNAALAAVI IHAVGDLITP PNTVYQFWRI SPFEVVIFFA
GVFVTIFSSI ENGIYTTVSI SAALYLFRAF KAKGRFMGRA KIHSVVGDHL LDRPEEFKRE
PSDRNSPKEG ESSVRQVFLP LGHDDGSNPL IELEDPYPGI FILRFSEGFV YLNANHYLDQ
LTETIFAKTR RTNPTAFNRP GDRPWNDPGP RRGKDVEVHE ELPTLKAIIL DMSSVNNVDL
TSIQNLIDVR NQLDKYAAPD TVDWHFSNIN NRWTKRALAA AGFGYYTPEP DNSGLHRWKP
IFSVAELGGS DSAAAAAEAK HNKRLQRSVS ERAADVEAGE GVRAVEDGSS EDGSLNKQLE
QSKAYSVGGL QSNKPSRKAV VQGLNRPLFH VDVTAALDSA LANAQRKSH
//