ID A0A2V1BND0_9HELO Unreviewed; 808 AA.
AC A0A2V1BND0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE SubName: Full=Sulfate permease {ECO:0000313|EMBL:PVH74878.1};
GN ORFNames=DL98DRAFT_467191 {ECO:0000313|EMBL:PVH74878.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH74878.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH74878.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH74878.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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|RuleBase:RU362052}.
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DR EMBL; KZ804211; PVH74878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1BND0; -.
DR STRING; 1485229.A0A2V1BND0; -.
DR Proteomes; UP000244409; 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:SF80; SULFATE PERMEASE 2; 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:UP000244409};
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..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 119..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 197..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 416..439
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 475..505
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 574..727
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
SQ SEQUENCE 808 AA; 89022 MW; 89F87045CBAE7B58 CRC64;
MPSTSDKVGH ALAKGLLIRT DYRKDATETL SRGESVISTS NAENYLEKEP TAADYFREIA
PNGQSVKTYF RDLFPFLNWI TRYNVQWLTG DVIAGLTVGA VVVPQGMAYA LLAKLPPEYG
LYTSFVGFIL YWAFATSKDI TIGTVAVMST LVGNIVIKVQ KTHPDIEAVE IARTLAVVSG
CVVLFIGLAR IGWIVEWISL TAITAFMTGS AITIGVGQIP ALLGIPGINN RGPAYEVFIN
TLKALPKARL DAAMGVSALF LLYFIRFGFE FLSRRYPARK KTFFFLSTLR IAFVLLLYIL
ISWLVNRGIK DAKKAHFKIL GKVPRGFQHA GAPTMNTRTI SAFASELPAT IIVLLIEHIA
ISKSFGRINN YIINPSQELV AIGFTNVFGP FLGAYPATGS FSRTAIKSKA GVRTPLAGVF
TAIVVLLALY ALTAVFFFIP MSSLAAVIIH AVGDLITPPN VVYQFWEVSP LEVPIFFIGV
FVTLFTNIEN GIYATIAASG ALLLFRLSKA KGRFVGRTKV QSLSQDSFSK LEARNASSSD
SEQSATLGHA RDVFLPLDRK DGSNPDIQVK QPHPGVFIYR FNEGFNYPNS QHYMEHFTEH
IFKETRRTTL DNYAKLGDRP WNDPGPRRGQ PAEVRTHLPI LRAVILDFSA VNNVDVSAVQ
NLVDVRNQLD RYASPATVGW HFANITSRWT RRALASAGFG YPKNNSPELN WKSIISVADF
DDSVSTINST SQEKARYDVE HQTKDDEITS DLAHRAAPAY DEKKGGNVTV TGKFVPLYGV
NRPFFHVDVF AAVEAALAVV EQDEAQQL
//