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Database: UniProt
Entry: A0A0L1J4V4_ASPNO
LinkDB: A0A0L1J4V4_ASPNO
Original site: A0A0L1J4V4_ASPNO 
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
//
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