ID A0A166FBA3_9AGAM Unreviewed; 865 AA.
AC A0A166FBA3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=SPX-domain-containing protein {ECO:0000313|EMBL:KZT40472.1};
GN ORFNames=SISSUDRAFT_1070196 {ECO:0000313|EMBL:KZT40472.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT40472.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT40472.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT40472.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KV428032; KZT40472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166FBA3; -.
DR STRING; 1314776.A0A166FBA3; -.
DR Proteomes; UP000076798; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd01115; SLC13_permease; 1.
DR CDD; cd14478; SPX_PHO87_PHO90_like; 1.
DR InterPro; IPR004680; Cit_transptr-like_dom.
DR InterPro; IPR001898; SLC13A/DASS.
DR InterPro; IPR004331; SPX_dom.
DR NCBIfam; TIGR00785; dass; 1.
DR PANTHER; PTHR10283:SF92; LOW-AFFINITY PHOSPHATE TRANSPORTER PHO91; 1.
DR PANTHER; PTHR10283; SOLUTE CARRIER FAMILY 13 MEMBER; 1.
DR Pfam; PF03600; CitMHS; 2.
DR Pfam; PF03105; SPX; 2.
DR PROSITE; PS51382; SPX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 399..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 478..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 525..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 608..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..678
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 684..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..302
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REGION 102..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 74..101
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 113..130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 96024 MW; 7A07A60186AA3A05 CRC64;
MKFSNSLKFN AVAEWWEEYI AYSALKKQIY QFEKQHTDWT RSGDDLEANQ PLMGPASTNE
AFTALLDREL TKIKSFYETQ EKELLDELED LSELVIQKET ESLASRSYSA PSVDEDDEDD
EDEDEPMDLP FDNDLNTPVS PRMKRQVSAN SGKRTRIIEP PKQSFPHDRR SSVSSSDNAD
LEASLSSLRN ASTERRKRAD SVVSTSSRGG KRRASLGHIL SLVVPSSSTA SNSVQGAPGT
VWTSNSDYAT DVRLLFKRRI TQLYIHLTSL KSYVELNHSG FRKILKKYDK VTLNELKDQY
LHEVVESAYP FLQSSRDRLS DGIARLIAMY AKCVTRGDHS AALRQLRVNQ REQIAWERDT
VWRQMIGKER RGESDGQVKT IGVIEDELRV ARSRFKKKHI FMLLAVVVFV ILLNVRMMDQ
VEANNCTAIL VFATILWATE AIPLFVTSIL VPLLLVCFRV VRSDTTHERL STPDATKYIF
SAMFSPTIML LIGGFTIASA LSKTSIDRIL ITRVLSLAGN KPRTVLLYFM GVACFASMWI
SNVAAPTLCF SLIQPILRTL PPKARFAPCL IIGIALAANI GGQCSPISSP QNLIALGYME
PAVSWPQWFA VSIPVAMVSI FLIWLLLLAS YRPGTTIDGE ALEIKPIRAA REPFTLKQYW
VTFVCIVTIA LWCAENSIKD LVGDMGVIAI IPIVAFFSTG VLKKDDFEQF LWTIVFIAMG
GIALGKAVTS SGLLEVMDHG IRRLISGLTL YTVVVVLSCV ILVISTFISH TIAAVLLVPI
AAEVGENMNV PHPRLLIFIT ALVCSTGMGM PVSGFPNQTA ATQEDEMGQL YLSNVDFLKN
GVPASIIATI VVFTIGFLIM QGLGL
//
