ID A0A2S5BGQ5_9BASI Unreviewed; 1056 AA.
AC A0A2S5BGQ5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=DUF221-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BMF94_1035 {ECO:0000313|EMBL:POY75951.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY75951.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY75951.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY75951.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(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:POY75951.1}.
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DR EMBL; PJQD01000009; POY75951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5BGQ5; -.
DR STRING; 741276.A0A2S5BGQ5; -.
DR OrthoDB; 366603at2759; -.
DR Proteomes; UP000237144; 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 PANTHER; PTHR13018:SF83; CALCIUM PERMEABLE STRESS-GATED CATION CHANNEL 1; 1.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR Pfam; PF14703; PHM7_cyt; 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:UP000237144};
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 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 639..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 701..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..200
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 271..491
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 502..773
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT REGION 339..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1021
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 117803 MW; DD8C9399D4267A45 CRC64;
MEGYLHLLVD SEPQNPGLPT GQLDKYRGPW FSTQLTLSLT VGVVSFLVFC WLRRYERFRV
LYAPRTMLKG FAPHEVHDHE SFFGFVLPTL RTSEFVVLQL VGLDAAVLLS FLRTGFYFFL
TCSVLAFALL VPVNWRENGT IEGVPPPPAN GTSTSYLDSL AFDALGQHGS RIQRGSTLYL
SAQLLFTYVF TILTIFYLRR AWRRYVPLRQ LFSLELAQSI PARTVMVTSL PPHLRSERAL
ADYFESIQLG PNSQSIGRDR RVAGSSSSEA VVPGLAVESV VVTRAIGSMR ELLERRTRAL
TTLEEAWSKY LGNPVPVEGK KAVFGYDRDV EVEAILHGPK DDVSGSAGTE GEGTAAGPAT
ARLVDVDGED EREPEGEAST EMRDPDQDVE ARLLPAARPS IVNPSQKRPR IRPHWFTKKV
DALDYYAEQF RLADEAVRRR RKGKFRPTGV AFVTFQTMAA AQVAAQTVHY PSPSEFHTEL
APEPRDIHWF NLNLSSTSVF IRHILVGLTL LLLLSVWSVP VAALASLLSW DTIHDVAPRF
AKLLGRSPRL RSFVQTTLPS LAMVAFNNVL PMFLEALSVF QGLPARSWIE LSQLKKYHLS
LLFTTLFVFI TTSTYTLLRD ISESPMKVLD KLATTLPDSR NFFVSYVMLA GLAIVPLQLL
ELATVIPRMF YQLFLTRTPR DHATLNAPTS LNLGVVYPQA LLIWTIGITY SIITPLILPF
AMLYFGLAYF VYKYRFLFVF YRPYESRGQA WPLAYNRVGL GLLIFQVFML GLFTVRKVFL
LVILMVPLVA GTAYAIWHIG KMYEPLSRYV NLSQACEVTS GEGSTDVTQL RKGHPVTKSQ
THLNRGRYGQ RGDGVYAVAK NPSTDYSQPP LSEMYPGVLN TGGSSRYGHP ALFGALPEPW
LPVVSEPSEA LPEVPQAVKD ALLVVDLRRG WRNLKRAAKH GISLGAGGGG GDAGVESGAS
EANQRRRRRA TGWGSLPSEE EDEDPSRAWR GSRESTPHHS QDGLDYDDEE NEDEDDDQDE
NGEPTSRYST FFPHRPRHGL QFPPTPGTAS ETEDEG
//
