ID A0A2J6SMU7_9HELO Unreviewed; 422 AA.
AC A0A2J6SMU7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Sec20-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=K444DRAFT_574975 {ECO:0000313|EMBL:PMD52040.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD52040.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD52040.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD52040.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KZ613912; PMD52040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6SMU7; -.
DR STRING; 1095630.A0A2J6SMU7; -.
DR InParanoid; A0A2J6SMU7; -.
DR OrthoDB; 1784161at2759; -.
DR Proteomes; UP000235371; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000235371};
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 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 141..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..101
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 151..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 46773 MW; E4905D3B8988C5A3 CRC64;
MSFQTLSERL TALQESNAQL KELIGRLATI KFQPGSIPLY NEEGNVITEL TSEIQQTLKD
QDEDLELLQE DVCDLDSGRH GSELEQQKDR LDQAVKRAVK ELKGCQTAFR RAQLTARRNL
QIAQRAEREL LLQSYLEPRS STALPMAGQQ RRRKEQNKEL SKEEKEVNAS TDVTLALRRT
HDMMTAELSR SQFAHDTLKE STAALAQLSE TYSALDTMLS RSRNLLGTLL TSQKSDTWYL
ETAFYILLAT IAWLVWRRLL YGPTWWILWF LPRTFFRGCF GILTFMGVIG GRKTDVGVSS
VAGGETVVHI SGTRGPKVAM AGQKAPSIQV GGGGKGGPAK ATGTLQGRPH EAAGDSVSEK
VGKIIDESGD APIEDEGAGS EKGTSDEEAK GEEVESQPNP KKRMWEEEKE SATEAKRKND
EL
//