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Database: UniProt
Entry: A0A2K0USL6_GIBNY
LinkDB: A0A2K0USL6_GIBNY
Original site: A0A2K0USL6_GIBNY 
ID   A0A2K0USL6_GIBNY        Unreviewed;       730 AA.
AC   A0A2K0USL6;
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=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753, ECO:0000256|PIRNR:PIRNR036956};
GN   ORFNames=FNYG_14538 {ECO:0000313|EMBL:PNP60778.1};
OS   Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP60778.1, ECO:0000313|Proteomes:UP000236664};
RN   [1] {ECO:0000313|EMBL:PNP60778.1, ECO:0000313|Proteomes:UP000236664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS10214 {ECO:0000313|EMBL:PNP60778.1,
RC   ECO:0000313|Proteomes:UP000236664};
RA   Gardiner D.M., Obanor F., Kazan K.;
RT   "Genome of Fusarium nygamai isolate CS10214.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PNP60778.1}.
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DR   EMBL; MTQA01000341; PNP60778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K0USL6; -.
DR   STRING; 42673.A0A2K0USL6; -.
DR   OrthoDB; 922060at2759; -.
DR   Proteomes; UP000236664; 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:UP000236664};
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          233..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..520
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..672
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..715
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  80194 MW;  765CBA92D9B9147F CRC64;
     MMSWWSSSAN TALDEQIEKA TSSSLEDIAL NLEISDVIRS KTVAPKEAMR SLKKRIGNKN
     PNTQLSALNL TDTCVKNGGS HFLAEVASRE FMDNLVSLLQ AVGGGAVNAD VKSKILELIQ
     SWAGATEGRY ELSYIGEVYR TLQRDGYQFP PKISVASSMI DSSAPPEWTD SDVCMRCRTP
     FTFTNRKHHC RNCGNCFDQQ CSAKVVALPH LGIMTPVRVD DGCYAKLTNK GHKIPNPSLD
     RSPTYPHKTR STSAMQPRNA RVDDGFDEDL KKALAMSLEE VKTHSHGYAG PAQTSYAANG
     DASAAKQAEE DDADLKAAIA ASLADMEEQK KRHAAALKEQ TSSSMDTSAT TNFVLPKNDY
     ELTPVEAENI NLFSTLVDRL QTQPPGTILR EPQIQELYDS IGTLRPKLAR TYGETMSKHD
     TLLDLHAKLS TVVRYYDRML EDRLSKAYSQ QNLGGYNLPP PRQAAGPYPS IPSQMPSNPA
     GAESFYTGQQ RASYQAPQHQ HYQQPPPHAT PQPQYPSYGS APEPQPGQYP RHQVQRADSW
     QNRAPSAPQD PYQQPQQPND HNLQTQNPQQ PQAPTASDPN ASYYFTPQQP QQTPLGPSAT
     GSAPDVNQSQ YPNLQQPSQY PGGSASAPSQ PTPGQAPAQV AQPGQPVQSP HMQHAQPPQP
     SQPQPPQPTQ QAPPQQQQAY WQPSMPQSHQ QPPVAPQNWA YGGYTQDSFP SVPQQEPAKQ
     PVKEEALIEL
//
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