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Database: UniProt
Entry: A0A066WXC6_COLSU
LinkDB: A0A066WXC6_COLSU
Original site: A0A066WXC6_COLSU 
ID   A0A066WXC6_COLSU        Unreviewed;       710 AA.
AC   A0A066WXC6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753, ECO:0000256|PIRNR:PIRNR036956};
GN   ORFNames=CSUB01_00626 {ECO:0000313|EMBL:KDN61543.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN61543.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
CC   -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC       receptor for ubiquitinated cargo proteins at the multivesicular body
CC       (MVB) and recruits ESCRT-I to the MVB outer membrane.
CC       {ECO:0000256|ARBA:ARBA00003067, ECO:0000256|PIRNR:PIRNR036956}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC       {ECO:0000256|ARBA:ARBA00011446, ECO:0000256|PIRNR:PIRNR036956}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004125,
CC       ECO:0000256|PIRNR:PIRNR036956}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004125, ECO:0000256|PIRNR:PIRNR036956};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004125,
CC       ECO:0000256|PIRNR:PIRNR036956}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the VPS27 family.
CC       {ECO:0000256|ARBA:ARBA00008597, ECO:0000256|PIRNR:PIRNR036956}.
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:KDN61543.1}.
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DR   EMBL; JMSE01001406; KDN61543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066WXC6; -.
DR   STRING; 1173701.A0A066WXC6; -.
DR   eggNOG; KOG1818; Eukaryota.
DR   HOGENOM; CLU_011862_1_0_1; -.
DR   OMA; DQQCSAK; -.
DR   OrthoDB; 922060at2759; -.
DR   Proteomes; UP000027238; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR   GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProt.
DR   CDD; cd15735; FYVE_spVPS27p_like; 1.
DR   CDD; cd21385; GAT_Vps27; 1.
DR   CDD; cd16979; VHS_Vps27; 1.
DR   Gene3D; 1.20.5.1940; -; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 6.10.140.100; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR017073; HGS/VPS27.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR002014; VHS_dom.
DR   InterPro; IPR049425; Vps27_GAT-like.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR47794; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR   PANTHER; PTHR47794:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF02809; UIM; 2.
DR   Pfam; PF00790; VHS; 1.
DR   Pfam; PF21356; Vps27_GAT-like; 1.
DR   PIRSF; PIRSF036956; Hrs_Vps27; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00726; UIM; 2.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50179; VHS; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|PIRNR:PIRNR036956};
KW   Membrane {ECO:0000256|PIRNR:PIRNR036956};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          26..150
FT                   /note="VHS"
FT                   /evidence="ECO:0000259|PROSITE:PS50179"
FT   DOMAIN          168..228
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          230..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..696
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   710 AA;  77731 MW;  CBF7BF06B691DE55 CRC64;
     MMGWWSSSAN TALDEQIEKA TSSSLEDIAL NLEISDVIRS KTVQPKEAMR SLKKRIGNKN
     PNTQLSALNL TDTCVKNGGA HFLAEIASRE FMDNLTSLLQ AVGPAAVNHE VKQKILELIQ
     SWAAATEGRH DLAYIGEVYK TLQREGHQFP PRISVASSMI DSSAPPEWVD SDVCMRCRTP
     FTFTNRKHHC RNCGNCFDQQ CSAKTCPLPH LGIMQPVRVD DGCYAKLTDK SAKGGAPLPQ
     DRSPTYPYKT RSTSAMQPRN ARVDDAFDED LKKALAMSLE EVKGYSQGYV APTTNGPSGP
     KVNGNSEPAA SNGADEEDAD LKAAIAASLA DMEEQKQRHA SALKEQTSSA GPSSTQQFSL
     PKNDYELTPV EAENINLFAT LVDRLQTQPP GTILREPQIQ ELYDSIGTLR PKLARTYGET
     MSKHDTLLDL HAKLSTVVRY YDRMLEERLS KAYSQHTVGG YNLPTPRGPS GAYPSLHASA
     PNSAGPAENF YTGSQQVDYG HAPPPQEYHQ HPQHAPQTQY ATYDKRASMA GPPTGSYPPQ
     DPQQTDNWRG GAGSAPDRQY TPQQPYAPSE PPQPGHQSYP GQPAGTPSTD PNASYYFNPQ
     QPSAPPSVLP AADSNSAPYP NLQQSMQYRQ SMSQQATPVQ AAAQPAQQQA PPQQQSYWQP
     SVPQQSAPSQ QHWQGQYNNN NNNVYTQESF PSAPQNAPKQ PAVEESLIEL
//
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