ID A0A316V6S1_9BASI Unreviewed; 865 AA.
AC A0A316V6S1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:PWN31893.1};
GN ORFNames=FA14DRAFT_162251 {ECO:0000313|EMBL:PWN31893.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN31893.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN31893.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN31893.1,
RC ECO:0000313|Proteomes:UP000245771};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.
CC {ECO:0000256|ARBA:ARBA00007779}.
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; KZ819606; PWN31893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316V6S1; -.
DR STRING; 1280837.A0A316V6S1; -.
DR InParanoid; A0A316V6S1; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000245771; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005227; F:calcium-activated cation channel activity; IEA:InterPro.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR003864; CSC1/OSCA1-like_7TM.
DR InterPro; IPR027815; CSC1/OSCA1-like_cyt.
DR InterPro; IPR032880; Csc1/OSCA1-like_N.
DR InterPro; IPR022257; PHM7_ext.
DR PANTHER; PTHR13018:SF143; PHOSPHATE METABOLISM PROTEIN 7; 1.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF12621; PHM7_ext; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000245771};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..865
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016407856"
FT TRANSMEM 36..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 635..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..186
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 212..405
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 416..693
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 789..856
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 749..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 96418 MW; 450D5F39484A99A1 CRC64;
MAVKMSNKAF LASAMVAFTM VNQAKAQSSS TNSSTSTVIS SLVLNLVIFT VEMTAFFILR
PKFPKIYRPK SYLGLESERV APTSDSLFGW IPEFLRTPTS VILYKNGLDA YQFVAFCEMM
IWFFVPVWLF TWIFLMPLYA ANSSIGAQGF NMFTYGNVGK SRSQQLRLIG VLFANWIIIL
YWIWVMRRFI ASFIKNRQEF LLSPEHRASA QARTILITGI PNDFLSERKL SNMYSHFPGG
VAKVWLNRDL QDMPDLFDQR MKACNKLEGA IASVQKIAFK KIKKGKVTAS TENKDAELDL
GVIEKYLTKK ERPTHKLGAM GCYGEKVDTL DWCREEIPRL TKELDERRRA AETDYETYRP
ASAAFIMFNT QIAAHMAVKT HAHHQPYRMA NHYLEAHPLD VIWENLGMNP YAVKIRTAIG
WAITIGLVLF WTLVTLVVGF ISNVTGTAEK ISWLHWLLTI PSVVRGIIQG ILPVVLLAVA
NILLVMFLRF LGRFSGIPTR SGVELSLFDR MAIFNIIQNF LILTIISGVS NGINQIVGVL
SKPAGLPGLL AQKVPNASTF FLSFVLLQGL TGCASGFLQI APLIIYYIKK FLLASTPRKL
WHIENDMPSV AWGTLFASTT LLSVIGIGYT IMAPIMNGFA MAAFMLLFVM YKYNFTYVYN
MSGATETAGL FFPKAINFCF AAMYLQMLIQ AVLFFISQYA YGGQSAIPEG VFMVILIVIT
IGFHYFFIDS YGSLYTALPL SLVQPEEGNV TGATSSNTPN EKKGLLSDTQ KGNAGIVDAN
SNRAASGTAA EHENGHEDPE DAFTPIPLKE NQRAIWIADD VLGLGRAENE RNRSAGISTT
MRGATRDDKG KIETDLHCPP GEILL
//
