ID A0A0B7NGE6_9FUNG Unreviewed; 496 AA.
AC A0A0B7NGE6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Anaphase-promoting complex subunit 4 WD40 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=PARPA_10738.1 scaffold 41684 {ECO:0000313|EMBL:CEP16472.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP16472.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP16472.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP16472.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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. It also functions as a component of the
CC nuclear pore complex (NPC). NPC components, collectively referred to as
CC nucleoporins (NUPs), can play the role of both NPC structural
CC components and of docking or interaction partners for transiently
CC associated nuclear transport factors. SEC13 is required for efficient
CC mRNA export from the nucleus to the cytoplasm and for correct nuclear
CC pore biogenesis and distribution. {ECO:0000256|ARBA:ARBA00025261}.
CC -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Component
CC of the nuclear pore complex (NPC). NPC constitutes the exclusive means
CC of nucleocytoplasmic transport. NPCs allow the passive diffusion of
CC ions and small molecules and the active, nuclear transport receptor-
CC mediated bidirectional transport of macromolecules such as proteins,
CC RNAs, ribonucleoparticles (RNPs), and ribosomal subunits across the
CC nuclear envelope. Due to its 8-fold rotational symmetry, all subunits
CC are present with 8 copies or multiples thereof.
CC {ECO:0000256|ARBA:ARBA00011369}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family.
CC {ECO:0000256|ARBA:ARBA00010102}.
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DR EMBL; LN733169; CEP16472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NGE6; -.
DR STRING; 35722.A0A0B7NGE6; -.
DR OrthoDB; 177928at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR11024; NUCLEAR PORE COMPLEX PROTEIN SEC13 / SEH1 FAMILY MEMBER; 1.
DR PANTHER; PTHR11024:SF3; NUCLEOPORIN SEH1; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 3: Inferred from homology;
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022927};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 9..41
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 344..389
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 443..474
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 177..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 55366 MW; 2C36CAA915095A3A CRC64;
MSSSLTKFDT GHEDLIHDIS YDFYGKRLVT CSSDQRLKVW DFVERPDASV WELNDAWKAH
DSSILKAIWA RPEYGQIVAS CSFDRQVKIW EEQTVEPRNS QKRWAERFRL VDARGAVLDI
AFAPSQDSLR LATCSSDGVV RIYEALEPTD LAQWSQMEEF EISSAYYQNS DAKFQSGISQ
IHHQQQQQQI QQQQQQNSQN GSHQAYNSHN SYQQQSQIPG YPYSSMNQLP QHPFGQQPVQ
TNSTSSSGSS IAGHGLSTPG VSDIPTMTST VQGVSPGSAT GIAGASAAVA SNVHRPIVAD
SGYCIDWCPN RTSTAMIAAG LGKEIGARIF KHDGHNRWIP SEFLPGHTQE VHDISWAPSM
ARSYQLIATA SKDNLVRIYK LTEQQQQQQQ QQQQQQTQQP QQPQQQQPQQ PQQRGRIPNS
PAGTPTQLGA TNKAYHIELI AAFDDHKAEV WKVEWNITGT ILSSSGDDGK LRLWTAGYDG
KWRQMAVITA NTQAHS
//
