ID   A1DII4_ASPF1            Unreviewed;      1251 AA.
AC   A1DII4;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   04-NOV-2026, entry version 115.
DE   RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1 {ECO:0000256|ARBA:ARBA00017923};
DE   AltName: Full=Class E vacuolar protein-sorting machinery protein hse1 {ECO:0000256|ARBA:ARBA00018978};
GN   ORFNames=NFIA_091500 {ECO:0000313|EMBL:EAW19191.1};
OS   Aspergillus fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Neosartorya fischeri).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW19191.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
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). {ECO:0000256|ARBA:ARBA00002654}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC       {ECO:0000256|ARBA:ARBA00011446}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004125}.
CC   -!- SIMILARITY: Belongs to the STAM family.
CC       {ECO:0000256|ARBA:ARBA00009666}.
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DR   EMBL; DS027696; EAW19191.1; -; Genomic_DNA.
DR   RefSeq; XP_001261088.1; XM_001261087.1.
DR   AlphaFoldDB; A1DII4; -.
DR   STRING; 331117.A1DII4; -.
DR   GeneID; 4587646; -.
DR   KEGG; nfi:NFIA_091500; -.
DR   VEuPathDB; FungiDB:NFIA_091500; -.
DR   eggNOG; KOG2398; Eukaryota.
DR   eggNOG; KOG3417; Eukaryota.
DR   HOGENOM; CLU_002632_0_0_1; -.
DR   OMA; AACCPCL; -.
DR   OrthoDB; 546434at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0007265; P:Ras protein signal transduction; IEA:TreeGrafter.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   CDD; cd11883; SH3_Sdc25; 1.
DR   FunFam; 2.30.30.40:FF:000072; Unconventional Myosin IB; 1.
DR   Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR   InterPro; IPR056685; DUF7783.
DR   InterPro; IPR056686; DUF7784.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR057827; WW_fungi.
DR   PANTHER; PTHR23113:SF368; CELL DIVISION CONTROL PROTEIN 25; 1.
DR   PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   Pfam; PF25006; DUF7783; 1.
DR   Pfam; PF25008; DUF7784; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF23518; WW_2; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48366; Ras GEF; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:EAW19191.1};
KW   Cell division {ECO:0000313|EMBL:EAW19191.1};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658,
KW   ECO:0000256|PROSITE-ProRule:PRU00168};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT   DOMAIN          82..142
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          811..944
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50212"
FT   DOMAIN          980..1216
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   REGION          30..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..184
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1251 AA;  140315 MW;  5081161A4D05335D CRC64;
     MYETRVTEPL AVDTRSALAT KTQTFATTFE FTDEQVSTPT SGPRRRSRGN SISVQQKGSP
     ERHRSPMKST SDGRYTPSPE PAPALFVRAM YDYDADDHTS LSFRRGDIIQ VLNQLETGWW
     DGVINNSVRG WFPSNYCAII TDPSELEDQV VHARDEDEIS AESAAGEDEY EEEHEHEHDE
     DEVDSAGNPR DSQPLLPIEG VAAPKEQEEA AFWIPQATPD GRLFYFNTLT GYSTMELPFE
     NPSANETGPF DRNNFFVPDQ TRPPPELMAR GFERDEDDYD GSASEAEGES LMLASHDSMS
     RRRRSYIDGV SPATSMDSLH PPSATKSINE GKISHQSSRD LQRTTASSNT SAAIHIHRPS
     ASSQAPSRFV DDGLTAPVTW PMLVDNMRHA IEVYRQTLLN GDRSEYVRKA EDISDHLRML
     LAAGSDTTDN HSGNPSIISQ NKPLYPHFRE MMSKFSKLVL SSHVAAADWP GPDSVNKCLQ
     EADGVMQGVY GYVEVARQQR GETIRRIVPG FVVGSSSGGG WQNNGVSLDD SGPTSFLDQD
     GADSRVEPSV PLDSALLDHI DILRRSFVGT IRRLEERLTL NQKKIVTYAE QREISDSVAA
     AAIKVVEQFR PWISAVESIN LAPLGTSFQN PQLVDFSLQK QRAYDAIADF VISCQAVSAP
     LGDEWAELRG DSLEDRLNAV RSIARQLENF VSQIGFSLSL LLEQIPEPST AFRSESRLEG
     DKEAYKGIHS RGDSLARIPT ETIGIPSSYS VDPPSEKVRR NMDKAQRFFG QAPPAAITRE
     PIREPVREPE ETPWFLKMDH EGEVFYDTKA DVPTLKCGTL AGLVEHLTRH DKLDASFNNT
     FLLTYRSFTT ASELFEMLAE RFNIQPPFGL NPDEMQMWID RKQKPIRFRV VNILKSWFEH
     FWMEPNDEAH MNLLARVHAF TKDSIATTKT PGSPQLMAVI EQRLKGQDTT VKRLVPTQAT
     AAPPPILPKN MKKLKFLDID PTEFARQLTI IESRLYSKIR PIECLNKTWQ KKVGPDEPEP
     ATNVKALILH SNQLTNWVAE MILTQSDVKK RVVVIKHFVN VADRCRALNN YSTLTSIISA
     LGTAPIHRLG RTWSQVSGRT SAILEQMRRL MASTKNFGEY RETLHLANPP CIPFFGVYLT
     DLTFIEDGIP SLTPSELINF NKRAKTAEVI RDIQQYQNVP YLLQPVPELQ DYILSNLQAA
     GDVHDMYDRS LEVEPRERED EKIARYAAAA SSRDLRSHST MAIASIVIAS R
//