ID A0A395RKB3_FUSSP Unreviewed; 1266 AA.
AC A0A395RKB3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RGP60570.1};
GN ORFNames=FSPOR_10537 {ECO:0000313|EMBL:RGP60570.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP60570.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP60570.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP60570.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(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 -!- 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:RGP60570.1}.
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DR EMBL; PXOF01000184; RGP60570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RKB3; -.
DR Proteomes; UP000266152; 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; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR PANTHER; PTHR13018:SF20; SPORULATION-SPECIFIC PROTEIN 75; 1.
DR Pfam; PF14703; PHM7_cyt; 2.
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:UP000266152};
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 74..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 739..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 786..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 960..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1032..1052
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..242
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 266..342
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 618..725
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 737..1017
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 1186..1257
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 142163 MW; 1D6AB2A9FD05512F CRC64;
MSSTETDASA SATGTGTETG TDSATGTASI TGSILSSLLS SAMTPSSTSG PTRTSGSLFE
SPTQSSAADK DKGIGIVSFL TAVGVAVAIF AVQILLFLIL RNKLARIFKP KTYLVPERER
TESPPSKPLA MLKTLWHYGD REVIEKCGLD AYFFLRYLKT LLIIFLPIGA VVMPILIPLN
YVGGLGQKID VTDDDEQSNE TPTGLDTLSW GNVAPKNSSR YGAHLLMAIL VVIWVCTVFF
FELRVYVKVR QDWLTSAEHR LRASATTVLV NSIPSKWLSE EALMGLFDVF PGGIRNIWLN
RDLSTLLDKV KERNNIHLQL EQAQTDLIKD AKKAQLKQQK AEEKKRRKEL KLKAMTKQER
ADKNALEDAE AQRRAQDGSG TAAGDQHNVP HSVDAGVRES QHDVFNRDSE DLHGHDHKKK
GFKVPLLGDP LAKVGQGILG VVSKAGNNVD ETIETTNGFV GLSQTTHSRN VSKSSNRGPE
RPSVDDDELN SPSDTLRVQN QSQNSMRRSG ESTAAMNPKP NQPLGNTVRK IDDIDEIYSK
EEAQWWQFWK PPPGAYASPV PQGDVSEAFR QKKTNESKPL WKRIKYALPF VSPEIEAEPL
EYPTAYNPDY DEAAEPAEWE KYLKKKDRPT HRLPLFGKSW LFPIPFVTKK VDTIYWCREQ
LARLNTEIEM DQQHPERFPL MNSAFIQFNN QVSAHMACQS VIHHVPRQMA PRVNEISPKD
VDWDNMAFSW WQEWLRSGIV FAIVIAMIFL WAIPVAWTAA LSQLDQLISS NEWLSFLKDN
EAVHNIAKAV AGVLPAVVLG LLLVLIPIFL DFLAGFRGAK TGAQRVEFVQ VFYFAFLFIQ
VFLIVSIASF FAASLDQLIH NVQELKTVSD VLDLLAVNLP SAANYFFSYM ILQAMSTSSA
TLLQLGALVM WYIIARILDS TARSKWSRNT SLRQVKWGAF FPIYTNFACI GLVYCVIAPL
IALFAIITFA LLWFAQRYAM LYVTRFEHDT GGVLYPRAIN QTFTGIYFME LCMAGLFFLV
EDENGEKVCA AHGVVMIVVL ILTILYQVLL NYSFGPLFRY LPITFEDEAV LRDQAFQRAQ
DQRLGLLDDD DLAEEPDKSY EKGAPTEKGI EMRRLASVRR PMKQVGTWAK DGGNQIAKFT
GVKQARDKNK RASEYRKKHR QKDVEAQLAI GEALFGGIHD EIEDLTPDER DALVRHAFQH
EALRARRPTV WIPHDDLGIS EDEIRRTQAY SEHIWISNEG TALDSKVRVV YGRAPPDFSE
IDLINL
//
