ID A0A2P5CNP1_PARAD Unreviewed; 397 AA.
AC A0A2P5CNP1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Target of Myb protein {ECO:0000313|EMBL:PON62635.1};
GN ORFNames=PanWU01x14_137500 {ECO:0000313|EMBL:PON62635.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON62635.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the TOM1 family.
CC {ECO:0000256|ARBA:ARBA00007708}.
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:PON62635.1}.
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DR EMBL; JXTB01000111; PON62635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5CNP1; -.
DR STRING; 3476.A0A2P5CNP1; -.
DR OrthoDB; 609735at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:InterPro.
DR CDD; cd03561; VHS; 1.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR044836; TOL_plant.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR46646; TOM1-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR46646:SF5; TOM1-LIKE PROTEIN 2; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF89009; GAT-like domain; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 3: Inferred from homology;
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 48..175
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 224..311
FT /note="GAT"
FT /evidence="ECO:0000259|PROSITE:PS50909"
FT REGION 310..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 44226 MW; 3A390B5BAF8CF737 CRC64;
MDKLKLAELG ERLKAGGAKM GRIVSGKVKE MKEILQTPTP ESTMVDEATL ETLEEPNWGM
NLRICTMINS EEFSGSEIVR AIKKKLSGKS VVSQRLSLDL LEDCTLNCEK VASEVASEKV
LEEMVRLIDD PQTDNGNRVR ATQLIRAWGE SEDLAYLPVF RQTYMSLKER GTPPSVQEGN
SLPVQYAVES FGQQPLSPPD RYPLPDSGLH DADGSAFPFN YQSLPGEEKK EFLVITRNSV
ELLSTILNSE TEPKPLKEDL TLSMLERCKE SQPVIKGIIE RTTDDEGMLF EALYLHDELE
RIISKYEELE CSEKSEERQQ LENSDSTKQE EESEFARKPG ETLPPKFDTE LERLEDANGG
GKQPDNFNGV SSSSQLGSPK ETKIVDSQQG GVPGSSI
//