ID V2XXJ3_MONRO Unreviewed; 678 AA.
AC V2XXJ3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 38.
DE SubName: Full=Endoplasmic reticulum protein {ECO:0000313|EMBL:ESK97250.1};
GN ORFNames=Moror_17906 {ECO:0000313|EMBL:ESK97250.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK97250.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK97250.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK97250.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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}.
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:ESK97250.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWSO01000030; ESK97250.1; -; Genomic_DNA.
DR RefSeq; XP_007843479.1; XM_007845288.1.
DR AlphaFoldDB; V2XXJ3; -.
DR STRING; 1381753.V2XXJ3; -.
DR KEGG; mrr:Moror_17906; -.
DR HOGENOM; CLU_003182_10_2_1; -.
DR OrthoDB; 6913at2759; -.
DR Proteomes; UP000017559; 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:0098661; P:inorganic anion transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
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; SULFATE TRANSPORTER; 1.
DR PANTHER; PTHR11814:SF263; SULFATE TRANSPORTER YPR003C-RELATED; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 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:UP000017559};
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 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 127..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 186..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 271..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 301..318
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 396..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 433..451
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 456..475
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT TRANSMEM 495..524
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362052"
FT DOMAIN 550..676
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 28..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 74610 MW; 5B8EC112496860D3 CRC64;
MAYPDLNSAP VSSSRSSLNI MGANDGLLTP RSVHSEETDH LLSAGGDIER GRVDQSSYGS
TSSSPEEGTK SRRSSKVKRR VQYYIPSIAW IPNYSFSLLG GDILAGFTVA SMLIPQSVSY
ASSLARLNPV TGLFSASIPG IIYAFLGTSR QLNVAPEAAL SLLLGQAVSD IHHDMDDRDK
GFPDSLGLSV ATVITLQVGF ISFLLGFFRL GFIDVVLSRA LLRGFIAAVA VVIMIEQLIP
MFGLVALEHQ IQPESTFDKL LFLIEHIWDH SHWETTIISF SALAILILAR SFKQVFKKYW
WIYRVPEVLV VVVVSTLLSD EFGWDQAGVD ILGDVPVKTG EGFFFQSPFK HSNLRFLKRT
TSTAVVISVI GFLDSIVAAK GAAAKFGYTV SPNRELVALG AANLAASFVP GTLPAYGSIT
RTRINGDVGA RTQMASLVCS GVILLATFFL LPWLYYLPKC VLASIILLVV FSLIAETPHD
VHYYWKMRSW IDLTLMTLTF VFSIIWNVEV GIVVSLIISL LLVVHRSSKA RMTILGRIPG
TDRWKPINEN PEAEEDVQGA VIVRLKENLD FANTAQLKER LRRLELYGVR KSHPSDRPSR
KEATSIVFHM ADVDSCDAIA AQIILELAEE YRNRGVGLIF THVQPPLRDT FEKAGIVKLL
GVDAFKENVA DAMSARAR
//