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Database: UniProt
Entry: A0A0D1YYK7_9PEZI
LinkDB: A0A0D1YYK7_9PEZI
Original site: A0A0D1YYK7_9PEZI 
ID   A0A0D1YYK7_9PEZI        Unreviewed;      1011 AA.
AC   A0A0D1YYK7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Sec23/Sec24 family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV09_03642 {ECO:0000313|EMBL:KIW05787.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW05787.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW05787.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW05787.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847537; KIW05787.1; -; Genomic_DNA.
DR   RefSeq; XP_016215656.1; XM_016356863.1.
DR   AlphaFoldDB; A0A0D1YYK7; -.
DR   STRING; 253628.A0A0D1YYK7; -.
DR   GeneID; 27311615; -.
DR   VEuPathDB; FungiDB:PV09_03642; -.
DR   HOGENOM; CLU_004589_1_0_1; -.
DR   InParanoid; A0A0D1YYK7; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000053259; 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:UP000053259};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          300..338
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          375..626
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          632..716
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          728..826
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          856..928
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  111213 MW;  28B9C0B859A47195 CRC64;
     MSDYSMYHAL GNQIPHDPNQ QPPPHSQPGS AGTRPPIVAG PAGYQQAGSV YGSVPAESYG
     SSSQPGYQQI PYQNQEHSQY GVQEHSGTGA TDGFSGLAHH MGSMTLGTDG SGTVRKKRRD
     RHAHHELQTT ASSQAFNGAL QPSTGQAQYG QTPFGQPQTP TPNPNQLPNL VNAQFLQNQQ
     AVREDHTARG TAVTSAQGRV DPEQIPSVPN SRDVPAQYYL ENVFATMDNH IAPPATVPFV
     AFDQGNSSPK FARLTMTHIP VSQEVLNSLG LPLGLVLQPL APLQDGEREI PVLDFGDLGP
     PRCRRCRAYI NPFMTFRSGG NKFICNMCTF PNDTPPEYFA PTDPTGVRVD RQQRPELTLG
     TVDFLVPKEY WTKQPVPLNL LFLIDVTEES VNKGFLTGFC EGIMNALYGG DPADETSPRL
     AKGAKVGIVA FDKQMHFFNL SSELEQAQMM VMPDIEDPFV PLSEGLFVDP HESKVAITQL
     LNQLPQMFNP DLHSGIKNPE PALLPALEAA ASALKSTGGK IICSLAALPT WGRGRLFLRD
     DNTAVAGTDA EKKLLTTEHP GYTKLANDMV SNGVGVDFFL AAPSGGYLDI ATIGHVSSKS
     GGEVYYYPNF HSPRDTLRLS KEIKHTVTRM TGFQALMKVR CSNGLQVSAY HGNFTHHTFG
     ADLEFGVIDA DKAIGVMFSY DGKLDPKLDA HFQSALLYTA ANGERRVRCQ NLVASVAETG
     GEAMKYVDQD AITTIIAKES AARIPERTLK DIRGAITEKT VDILANYRKH FSSAHPSGQL
     VIPENLKEFG MYMLSLIKTR AFKGGREPSD RRVHDLRLLR SMGALETSLY LYPRIYSIHN
     LADMDGFPNE NGHLRMPLSL RASFSKMEEG GAYIVDNGQI CLLWLHAHVS PNLLEDLFGP
     GITDLKDLDP FMNQLPVLET HLNAQVRNIL QYLETVRGSK ALTIQLARQG LDGAEYEFAR
     LLVEDRNNEA QSYVDWLVHL HRQIQMELSG QRKKEESEHS TFMGLRGQYF G
//
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