ID   VPS27_NEOFI             Reviewed;         729 AA.
AC   A1DFP5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Vacuolar protein sorting-associated protein 27;
GN   Name=vps27; ORFNames=NFIA_081460;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027696; EAW18202.1; -; Genomic_DNA.
DR   RefSeq; XP_001260099.1; XM_001260098.1.
DR   AlphaFoldDB; A1DFP5; -.
DR   SMR; A1DFP5; -.
DR   STRING; 36630.CADNFIAP00007459; -.
DR   EnsemblFungi; EAW18202; EAW18202; NFIA_081460.
DR   GeneID; 4586655; -.
DR   KEGG; nfi:NFIA_081460; -.
DR   VEuPathDB; FungiDB:NFIA_081460; -.
DR   eggNOG; KOG1818; Eukaryota.
DR   HOGENOM; CLU_011862_1_0_1; -.
DR   OMA; SDMVRSK; -.
DR   OrthoDB; 828765at2759; -.
DR   Proteomes; UP000006702; 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   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; 2.
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..729
FT                   /note="Vacuolar protein sorting-associated protein 27"
FT                   /id="PRO_0000292519"
FT   DOMAIN          16..147
FT                   /note="VHS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT   DOMAIN          261..280
FT                   /note="UIM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   DOMAIN          307..326
FT                   /note="UIM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   ZN_FING         165..225
FT                   /note="FYVE-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          276..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..564
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   729 AA;  79654 MW;  662C82CE45615DA9 CRC64;
     MAGWFSSTSL LDEQVERATS SSLEDIALNL EISDLIRSKS VQPKEAMRSL KRRLENRNPN
     VQIATLKLTD TCVKNGGSHF LAEIASREFM DNLVSLLTTE GAPLNTDVKE KMLELIQDWA
     MAAQGRMDLN YLGETYRRLQ SEGFRFPPKN EISGSMLESS APPEWIDSDV CMRCRTPFSF
     MNRKHHCRNC GNVFDAQCSS KTLPLPHLGI LQPVRVDDGC YAKLTSKSSL PSNLSDRSAF
     KNHSITKANA MEPRGARAEG GFDDDLRRAL QLSLEEAQNK GSSGYVPSTR INDEPAKTTT
     QANHEEEEDA DLKAAIEASL RDMEEHKKKH AAALKSNAAA TDSSARDTTA ATPLPKNPYE
     LSPVEVENIH LFAALVDRLQ HQPPGTILRE PQIQELYESI GALRPKLARS YGETMSKHDT
     LLDLHAKLST VVRYYDRMLE ERLSSAYSQH SLGYGTVPGG SPYPNMYPTM PSHVPEGKTG
     AENFYYGNPV ADRAPPVNNT YGYPQSSRDI REPAAAPSGP ISSGMYNQPS QAVPQNPPWN
     GNAPSVASPQ PSAPSTPFPN NPSGYPGPSA STQYYASAPH PEQDPNAYSS PRPGETDISH
     QPSPIMRRDS YYQSAGAPVT ARASAPEQSP PTDQGQSPAY MQYGDSHPVQ STGQPTPQYQ
     PTAPPPQSYY FQHQPQQSAP LPTHSQTPGA PHGTYPGGDV SPISAPAHAV HYQQVAPTKP
     AVEESLIEL