ID A0A2S5B2F3_9BASI Unreviewed; 1164 AA.
AC A0A2S5B2F3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:POY70963.1};
GN ORFNames=BMF94_6025 {ECO:0000313|EMBL:POY70963.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY70963.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY70963.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY70963.1,
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: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004211}.
CC -!- SIMILARITY: Belongs to the SEC20 family.
CC {ECO:0000256|ARBA:ARBA00037934}.
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:POY70963.1}.
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DR EMBL; PJQD01000093; POY70963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5B2F3; -.
DR STRING; 741276.A0A2S5B2F3; -.
DR OrthoDB; 1709334at2759; -.
DR Proteomes; UP000237144; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
DR InterPro; IPR005606; Sec20.
DR PANTHER; PTHR12825; BNIP1-RELATED; 1.
DR PANTHER; PTHR12825:SF0; VESICLE TRANSPORT PROTEIN SEC20; 1.
DR Pfam; PF03908; Sec20; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT REGION 22..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 81..115
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 361..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..508
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..600
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..883
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1156
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 123710 MW; 0F587D1F80F9A168 CRC64;
MFCRSLVISF DSDHNHIRLM PPPAHTPAPA ALRAPPAPPT LPGDFQDAAT AIERRLVDVE
QYQVPQLAEC RGPLSFHNEL ATAIRQELAR ARRDLDELKV EADDLDRAKE RVAASQLIAS
IQQRLDSCTR AYRQAVVASK RQIDASAHLV AREELFASTS GRGSPAPGAG GSARAKSPMP
GQGGDDALMQ ATSDVTEGLR RTLQLMQQEI DRSMVSNELL ESQTQTMQLT SNQYSTLSSL
MNTSKNLITT LERSNILDRL VLFGAFAFFA AVCAHIFKKR VIDRGVHGVG ALGGIVAKGG
GAVAGLASKA QTSDAIAEEA TQVVKRGVAD EWARATAAAA GAAGAVRAGI DMARSKANQV
VTDRDVPTQT PSLVDSARHP SPPQRDAFEE AVPFEEEPFT APVQSETDSD ADSVIDEMTD
SARESVRIVE DDTSLEEPVA TAAVSDEPLK PAVVEPLDDH YDDTVSDEDG YPASDEESYD
SEDLQSATGI DNDDDDADND DDDEVTFPEA HEAETVAPRQ PHPPTPSLPD ILDLAFETPN
AEEPPARMPD LQDDALSMDS GVALGGDDDH ATKFDVEEDW SDEGEGLIDP IVEGDPETSA
DTEGETTVGG FQPDPVEAEA ASDPEEFEEE LVALDVAGVV GQDSASTSAE PLPSEPLQLL
DLDLPTDYSD LDLDAAPEYV WPVDYESTLQ AEPLDGIEVQ SLPRDVAGVE GTTRPLDIVT
EEDAPPPLDV EELGFVPASD ATEIGGQAVS ADLPIDLDTE QTIWSDSTAT KSLGDESAHY
LDDVTTDNVP YEEVEQADES LLEAILEQQM GYAAGPGAFG DRPDFQDAER DGTGEALSGP
VDTEGATSSL PEEVAPDLPP ASEGRALLGD DEDEDDDEED DHDPAEMASV HEASTYASTI
APTDEPTAPA TSEDLARTMP PASPHAASTS TSPDAAASVD ADDLPPSPTD PLEPAAPAAP
VSAPEGAAVR SSAPPPEENH ADEGAQSRSH RATEAAQTPA SSPTHDTAQL EEPLLQQPEL
SDELELASAP EDSLVPTHAE AEIVEHGTGQ ADAHLDEIIE PSADYWEPEN VLAADPIAVS
TYDDDLELPE SIPQTAYDRD FVEDIDEVLG SDLAPNEEGE TSERHAEDVD RTPRGEETSA
PAEDAAEDEL DDFADDEDGI VRML
//
