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VPS27_MAGO7
ID   VPS27_MAGO7             Reviewed;         713 AA.
AC   A4QTV1; G4N3H2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Vacuolar protein sorting-associated protein 27;
GN   Name=VPS27; ORFNames=MGG_04958;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- DOMAIN: The FYVE domain is involved in the binding to
CC       phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the
CC       association to endosomal membranes.
CC   -!- DOMAIN: Both IUM domains are necessary for efficient binding to
CC       ubiquitin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS27 family. {ECO:0000305}.
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DR   EMBL; CM001233; EHA52647.1; -; Genomic_DNA.
DR   RefSeq; XP_003712454.1; XM_003712406.1.
DR   AlphaFoldDB; A4QTV1; -.
DR   SMR; A4QTV1; -.
DR   STRING; 318829.MGG_04958T0; -.
DR   PRIDE; A4QTV1; -.
DR   EnsemblFungi; MGG_04958T0; MGG_04958T0; MGG_04958.
DR   GeneID; 2675537; -.
DR   KEGG; mgr:MGG_04958; -.
DR   VEuPathDB; FungiDB:MGG_04958; -.
DR   eggNOG; KOG1818; Eukaryota.
DR   HOGENOM; CLU_011862_1_0_1; -.
DR   InParanoid; A4QTV1; -.
DR   OMA; PHSSCYS; -.
DR   OrthoDB; 828765at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
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   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR017073; HGS/VPS27.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR002014; VHS_dom.
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   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF02809; UIM; 2.
DR   Pfam; PF00790; VHS; 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; SSF48464; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50179; VHS; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..713
FT                   /note="Vacuolar protein sorting-associated protein 27"
FT                   /id="PRO_0000292518"
FT   DOMAIN          18..150
FT                   /note="VHS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT   DOMAIN          274..293
FT                   /note="UIM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   DOMAIN          324..343
FT                   /note="UIM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   ZN_FING         168..228
FT                   /note="FYVE-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          230..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  78060 MW;  927DAFA0410D255E CRC64;
     MMSWWSSGAN TALDEQIEKA TSSSLEDIAL NLEISDVIRS KTVPPKDAMR SLKKRIGHKN
     PNTQLSALEL TDTCVKNGGQ HFLVEIASRE FIDNLVSLLK ATGPAAVNAD VRARILGLIQ
     SWAAVTQGRV ELSYIGEVYK TLQHEGFQFP PKVAVATSMI DSSAPPEWTD SDVCMRCRTP
     FTFTNRKHHC RNCGSCFDQQ CSSKSIPLPH LGIMQPVRVD DGCYAKVTDK SRGSGGAGAG
     AGYDRKSPSL YSSFPHKNRS SSAMQPRSAR VDDGFDEDLK KALAMSLEEV KSHSRNYAPA
     SNGVANSGQS KVNGDSSATK TVEEEDDDLK AAIAASLADM EEQKKKHSAV LHEQTHSTEA
     ASASTFVPPK NDYELTPVEA ENINLFATLV DRLQTQPPGT ILREPQIQEL YDSIGTLRPK
     LARTYGETMS KHDTLLDLHA KLATVVRYYD RMLEERLSKA YGQRNFAGYN MHVPRQTSSP
     YPSLQGPSAP ANVPGESFYT GQPQHDYAEP SRQPSYPPQA SGAQQQFHQY APPHQASQPS
     EGWQPSHTPA PAAQYAGQPP QQSTESTHSH SSAHNHQNLA APSAPDQSLP TPTTDPAASY
     YFNQQQVSAL QTPVSVPAEP VQSPYPNLQQ QPPAQYQHSP APQGQAQQQK PPQQPQQPYW
     QHSASQNTAL PTNHQPWPQV PNRQSASYVQ EPLPSAPQHA PQKPVVEEAL IEL
 
 
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