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Database: UniProt
Entry: A0A1Y2VUN8_9PEZI
LinkDB: A0A1Y2VUN8_9PEZI
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ID   A0A1Y2VUN8_9PEZI        Unreviewed;      1004 AA.
AC   A0A1Y2VUN8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTB00621.1};
GN   ORFNames=M426DRAFT_65524 {ECO:0000313|EMBL:OTB00621.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB00621.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB00621.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB00621.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC       promotes the formation of transport vesicles from the endoplasmic
CC       reticulum (ER). The coat has two main functions, the physical
CC       deformation of the endoplasmic reticulum membrane into vesicles and the
CC       selection of cargo molecules. {ECO:0000256|ARBA:ARBA00025471}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008334}.
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DR   EMBL; KZ111595; OTB00621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2VUN8; -.
DR   STRING; 1001833.A0A1Y2VUN8; -.
DR   InParanoid; A0A1Y2VUN8; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000242955; Unassembled WGS sequence.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR   Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR012990; Sec23_24_beta_S.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR   PANTHER; PTHR13803:SF4; SECRETORY 24CD, ISOFORM C; 1.
DR   Pfam; PF00626; Gelsolin; 1.
DR   Pfam; PF08033; Sec23_BS; 1.
DR   Pfam; PF04815; Sec23_helical; 1.
DR   Pfam; PF04811; Sec23_trunk; 1.
DR   Pfam; PF04810; zf-Sec23_Sec24; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR   SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          299..337
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          377..624
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          631..715
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          727..830
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          858..902
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..72
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1004 AA;  109244 MW;  F512FF96BC7D1A47 CRC64;
     MADYSMYHSL GQGEQLDPND PNRTTQPAPQ QFQPPIATNP YQQNPAYGSP VPGQQYYGNP
     PPGGPSPVAP GFAPPQDGGL ASQMAGMSIR DGQASVRKNK KKDRHVFHSV EAPAGSSQPY
     NGIPPVGTPA TAFLNADPST QIGGQFIGQP VSPNQFPAAV NAPYQPGTPA TAAEFAARGG
     QLDSGQSPTF VPAAGGGQVS PDDIPSVPVS RDVPQQYYLT NQYPTFERHV PPPATVSFVA
     WDQGNSSPKF TRLTMNSIPA NAEGLKSTGL PLGLVLQPLA GLQPGEMEVP VLDFGDVGPP
     RCHRCRAYIN PFMMFRSGGS KFVCNLCTYP NDTPSEYFCA TTPQGVRVDR DQRPELTRGT
     VEFTVPKEYW TKEPTGLHWL FAIDVTQESY NKGFLEAFCE GILAALYAPE DGEETDENGE
     LKRRIPPGAK VGFVTYDKDI HFYNCNPALE QAQMMIMPDI EDPFVPLSDG LFVDPYESKA
     VITSLLARLP TLFSDIKNPE PALLPTLTSC LAALEKTGGK VIASLSALPT WGPGRLFMRD
     DGKYSSGEMD KKLFSTEHPA WRKTAEKMVA AGVGVDFFLA APSGGYLDIA TVGHISATTG
     GETFYYPNFV AGRDNAKLSL EIKHTVTRET GYQALMKVRC SNGLQISGYH GNFIQHTFGA
     DLEIGVIDAD KAVGVTFGYD GKLDSKLDAH FQSALLYTTA SGERRVRCCN VIASVSDNPR
     ECMKFVDQDA VYTIIAKDAA SKLASTSSTL KDIRLGLTEK TIDILAGYRK NFSSQSHPPG
     QLVMPEKLKE FAMYMLGLIK SRAFKGGNET SDRRVHEMRM IRSIGAPELS LYLYPRMIPI
     HNLNPEDGFA DAQTGQLKVP PAIRASFSRV EPGGVYLVDN GQQCLLWFHS QTSPNLLVDL
     FGEGKDSLNS LDPYSSSLPV LQTHLNAQVR NILEFLKTVR GSKALTIQLA RQGIDGAEYE
     FARMLIEDRN NEAQSYVDWL VHIHKGVQLE VSSPPVLFAL AVTS
//
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