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Database: UniProt
Entry: A0A0C9SWZ5_PLICR
LinkDB: A0A0C9SWZ5_PLICR
Original site: A0A0C9SWZ5_PLICR 
ID   A0A0C9SWZ5_PLICR        Unreviewed;       595 AA.
AC   A0A0C9SWZ5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Eukaryotic translation initiation factor 2D {ECO:0000256|ARBA:ARBA00013816};
DE   AltName: Full=Ligatin {ECO:0000256|ARBA:ARBA00030186};
GN   ORFNames=PLICRDRAFT_57876 {ECO:0000313|EMBL:KII84045.1};
OS   Plicaturopsis crispa FD-325 SS-3.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Amylocorticiales; Amylocorticiaceae; Plicaturopsis.
OX   NCBI_TaxID=944288 {ECO:0000313|EMBL:KII84045.1, ECO:0000313|Proteomes:UP000053263};
RN   [1] {ECO:0000313|EMBL:KII84045.1, ECO:0000313|Proteomes:UP000053263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-325 SS-3 {ECO:0000313|EMBL:KII84045.1,
RC   ECO:0000313|Proteomes:UP000053263};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Translation initiation factor that is able to deliver tRNA to
CC       the P-site of the eukaryotic ribosome in a GTP-independent manner. The
CC       binding of Met-tRNA(I) occurs after the AUG codon finds its position in
CC       the P-site of 40S ribosomes, the situation that takes place during
CC       initiation complex formation on some specific RNAs. Its activity in
CC       tRNA binding with 40S subunits does not require the presence of the
CC       aminoacyl moiety. Possesses the unique ability to deliver non-Met
CC       (elongator) tRNAs into the P-site of the 40S subunit. In addition to
CC       its role in initiation, can promote release of deacylated tRNA and mRNA
CC       from recycled 40S subunits following ABCE1-mediated dissociation of
CC       post-termination ribosomal complexes into subunits.
CC       {ECO:0000256|ARBA:ARBA00025522}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the eIF2D family.
CC       {ECO:0000256|ARBA:ARBA00010359}.
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DR   EMBL; KN832572; KII84045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9SWZ5; -.
DR   HOGENOM; CLU_012487_1_1_1; -.
DR   OrthoDB; 102595at2759; -.
DR   Proteomes; UP000053263; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IEA:InterPro.
DR   CDD; cd11608; eIF2D_C; 1.
DR   CDD; cd11610; eIF2D_N; 1.
DR   CDD; cd21156; PUA_eIF2d-like; 1.
DR   Gene3D; 3.10.400.20; -; 1.
DR   Gene3D; 3.30.780.10; SUI1-like domain; 1.
DR   InterPro; IPR039757; EIF2D.
DR   InterPro; IPR048247; eIF2D_N.
DR   InterPro; IPR039759; eIF2D_SUI1.
DR   InterPro; IPR041366; Pre-PUA.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR048248; PUA_eIF2d-like.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   PANTHER; PTHR12217; EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; 1.
DR   PANTHER; PTHR12217:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 2D; 1.
DR   Pfam; PF17832; Pre-PUA; 1.
DR   Pfam; PF01472; PUA; 1.
DR   Pfam; PF01253; SUI1; 1.
DR   SUPFAM; SSF55159; eIF1-like; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS50296; SUI1; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053263}.
FT   DOMAIN          389..480
FT                   /note="DM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51925"
FT   DOMAIN          505..578
FT                   /note="SUI1"
FT                   /evidence="ECO:0000259|PROSITE:PS50296"
FT   REGION          209..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  63898 MW;  603E88D755F590EB CRC64;
     MFKKPLAHLK TSAPLRSSDR RKLKQRALQT FAIPAEEGDA LVPDGLLAVK FSTHLDEPGV
     AYLSPDGDPL WFTLGIGKEA EDLIPTVYTL WKRPTLLPFL STPSAVIPVL VGGADLMIPG
     VVECAPDLSP GRLVSITQYA GPGKRGPPLA VGRMVVSSGE LIGDEGGGIE GEGRKGKAVR
     VLHTWKDHLW EVGKGGDVPE VVVVNDGQVD GGEASAEGER GPGEGGGVEE SGESANGVLS
     GEAQSPPLSP QEVSTILRTS LLQALSTTLS ALPHSALPLP APAFYSTYIL PARPYHPPPS
     ASSTPIDIKH SAFKSLSAFL KSTEKDGLLK LKETKADGLV VVGVSPKHAE VAGHRGYVTI
     KDIETKRERA EKREKERERE GKGEMEVTEL WKPWQGSVAF FDGVGKETTK LYAHPELKSI
     LNEYITAQHL VNPREQQYVN VDALLRSFLV AKSKPKPGAE PEPPLEFIKR EEILAKLLER
     MQPWHEIRVD AKEPSSPKKG ALKPISVVTK IRQGRKASTL IAGFEPFGLE ANFLAEELRH
     ACASATSVSP IAGKGSALEV LVQGKQIKAV TELLASQGVP RKWVAAADLG DGKKR
//
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