ID A0A0L1J4V4_ASPNO Unreviewed; 1491 AA.
AC A0A0L1J4V4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Vacuolar protein sorting-associated protein 27 {ECO:0000256|ARBA:ARBA00017753};
GN ORFNames=ANOM_004763 {ECO:0000313|EMBL:KNG86772.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG86772.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG86772.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG86772.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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}. 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}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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:KNG86772.1}.
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DR EMBL; JNOM01000103; KNG86772.1; -; Genomic_DNA.
DR RefSeq; XP_015407695.1; XM_015550020.1.
DR STRING; 1509407.A0A0L1J4V4; -.
DR GeneID; 26806567; -.
DR OrthoDB; 922060at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProt.
DR CDD; cd02922; FCB2_FMN; 1.
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; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR003710; ApbA.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR47794; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR PANTHER; PTHR47794:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 27; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF00790; VHS; 1.
DR Pfam; PF21356; Vps27_GAT-like; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00726; UIM; 2.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
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 24..147
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 165..225
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 730..789
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 808..1165
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT REGION 276..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1491 AA; 163917 MW; 3E25BD03D834EC4C CRC64;
MAGWFSSSSP IDDQVEKATS SSLEDIALNL EVSDLIRSKS VQPKDAMRSL KRRLENKNPN
VQLATLKLTD TCVKNGGTHF LAEIASREFM DNLVSLLKAD GSPLNTEVKE KMLELIQDWA
MAAQGRMDLS YVGETYRKLQ DEGFRFPPKT QISGSMLESS APPEWIDSDV CMRCRTPFSF
MNRKHHCRNC GNVFDAQCSS KSLPLPHLGI LQPVRVDDGC YAKLTSKPFT PSGLSDRSAF
KNNSITKSTV MEPRTARAEG GFDDDLRRAL QMSLEEAQGR GSTGYVPQPK VTQEPPQASS
QSRIEEEEDA DLKAAIEASL RDMEQHKQKH AAALKNTPTT EPSTSRDAPG ATSLPKNPYE
LSPVEVENIH LFSTLVDRLQ HQPPGTILRE PQIQELYESI GTLRPKLARS YGETMSKHDT
LLDLHAKLST VVRYYDRMLE ERLSSAYSQH SLGYGTVPSG PRYPNVYPPM PQHASEGKSG
VENFYYGNTG AEKPPVSGTP YTQQQPEGEG LERTGMRSGA MSPGMYSQPP PAMPQNLPWH
GKAQAASPQI SAANTPYPQS PSAYPAPGAP THFYTTSNQP EQDVNPYQPP RQSEVDTSYM
PSPVTRRDSL YQPAAHSNVS APSVPEQPPS AEQMAYLHLS ESHPMQPGSQ PTLHHQPTDP
AAQSYYYQQQ PPPAHPATAY SQGQPTYHGA YPVNDASPVG GTAPPTQYQQ PPPSRPAVEE
SLIELSFKTG NSTQINDFVD AHPGGPNVIL RCAGKDATKD FDSVHELEIL TQSLAPSALR
GHIEPGTLEK SNDIHEMNSP NKDASLPPPL SSLLNLHDFE IVAQKHLPPN AWAYYASGAE
DEISKRQNSK AFQKVSLRPR ILRSIPTVDT TTNILGKQVS LPVYMSAVGI AKLAHPDGER
ALAAAAGKEG LAQVLANGAN NVIESVMDAR TSPEQPIFQQ LYVNRDITKS EDVVRRAERA
GVSAIWITVD SPVVGKREMD ERLNLQVEAR DDPSRKGQGV AKTMASFISP FIDWDILSWL
RGLTKLPIVI KGIQCVEDAV RAYHSGVQGI VLSNHGGRSQ DTAQAPLLTH LEIRRYAPFL
IDSKMQIFID GGIRRGTDVL KAVALGATAV GLGRPTLYSL AAGYGEQGAR RAIEILRQEI
ESNMIFLGVR NLKELGPHLL NTARLERDVV GMSNQIDILL YGLGAIGSFY AFILTRNDRV
RLTVVARSNY DAVKGDGIFL DSGNHGQHRF RPHQVIKSLD EVSGPFDYVV CAHKAIDQEA
VVARLQPAVN ERTTIVIIQN GVGNEEPFRS TFPMSSIITC VTWVGATQTS PGTVKHTKSE
DMQIGLFPNT SVDETLERTR LNTFASLLEG GGTKFQVLED MQRQRWEKVV WNAAWNPITT
LTLLDTQSWL HSSKDATPLT RRLMREVIDV GRRCGVPLEY GLVDELMDRI NSLPGVGSSM
QTDYKNGRPM EVDVILGFPA RKAKEFGMET PVLDTIHALV RAVDGRVRAA L
//