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Database: UniProt
Entry: A0A109FH91_9BASI
LinkDB: A0A109FH91_9BASI
Original site: A0A109FH91_9BASI 
ID   A0A109FH91_9BASI        Unreviewed;       417 AA.
AC   A0A109FH91;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Vacuolar fusion protein MON1 {ECO:0000256|ARBA:ARBA00018132, ECO:0000256|RuleBase:RU367048};
DE   Flags: Fragment;
GN   ORFNames=RHOSPDRAFT_18140 {ECO:0000313|EMBL:KWU44365.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44365.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU44365.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU44365.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for multiple vacuole delivery pathways including the
CC       cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and
CC       endocytosis. {ECO:0000256|RuleBase:RU367048}.
CC   -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC       {ECO:0000256|RuleBase:RU367048}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU367048}. Prevacuolar compartment membrane
CC       {ECO:0000256|ARBA:ARBA00004380, ECO:0000256|RuleBase:RU367048};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004380,
CC       ECO:0000256|RuleBase:RU367048}. Vacuole membrane
CC       {ECO:0000256|RuleBase:RU367048}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU367048}.
CC   -!- SIMILARITY: Belongs to the MON1/SAND family.
CC       {ECO:0000256|RuleBase:RU367048}.
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DR   EMBL; KQ954480; KWU44365.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FH91; -.
DR   STRING; 1305733.A0A109FH91; -.
DR   OrthoDB; 73361at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-UniRule.
DR   GO; GO:0006623; P:protein targeting to vacuole; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR043972; FUZ/MON1/HPS1_longin_1.
DR   InterPro; IPR043971; FUZ/MON1/HPS1_longin_2.
DR   InterPro; IPR043970; FUZ/MON1/HPS1_longin_3.
DR   InterPro; IPR004353; Mon1.
DR   PANTHER; PTHR13027; SAND PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13027:SF7; VACUOLAR FUSION PROTEIN MON1 HOMOLOG; 1.
DR   Pfam; PF19036; Fuz_longin_1; 1.
DR   Pfam; PF19037; Fuz_longin_2; 1.
DR   Pfam; PF19038; Fuz_longin_3; 1.
DR   PRINTS; PR01546; YEAST73DUF.
PE   3: Inferred from homology;
KW   Autophagy {ECO:0000256|RuleBase:RU367048};
KW   Endosome {ECO:0000256|RuleBase:RU367048};
KW   Membrane {ECO:0000256|RuleBase:RU367048};
KW   Protein transport {ECO:0000256|RuleBase:RU367048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW   Transport {ECO:0000256|RuleBase:RU367048};
KW   Vacuole {ECO:0000256|RuleBase:RU367048}.
FT   DOMAIN          6..126
FT                   /note="FUZ/MON1/HPS1 first Longin"
FT                   /evidence="ECO:0000259|Pfam:PF19036"
FT   DOMAIN          169..241
FT                   /note="FUZ/MON1/HPS1 second Longin"
FT                   /evidence="ECO:0000259|Pfam:PF19037"
FT   DOMAIN          308..404
FT                   /note="FUZ/MON1/HPS1 third Longin"
FT                   /evidence="ECO:0000259|Pfam:PF19038"
FT   REGION          246..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KWU44365.1"
SQ   SEQUENCE   417 AA;  45686 MW;  1C89B6A07C394317 CRC64;
     YLPRRYFILS TAGKLVYTSD TSEEAATGLV GVMQAIISIF ADEGDKIRYI DVGQTKISFL
     LKAPLYLVVV SSQGEPETVL RQHLDYLYLQ VLSVVTVSQL QNIFAKRSNF DLRQLISGTE
     PFFDSLVSTL QTSLAVALSS ISVYRLPPTL RSDLARALDP GKETIRSLDL LYVLLLAEGR
     LVTLLRPKKH SIHPTDLHLL LETVRRPSPL LEPGAESWFP ICLPRFNPRG FLHAYVSFLE
     TSPTSPPHSL SASSSGSNES KAGGGGGGGA KAEDGIGVVI LTDGGLVHSI LMSRAHQSYS
     LGELAIPGLR HFVYKDRERV QVTTPRWEGE LMTLYQRLHA ALHPRTNASG GGGASVQYLR
     TSHEAVLGWM TNDFELYVST SPLLPPAAMV KCARRVSEWV KRDEARLFLS GKGAGVF
//
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