ID A0A1Y1JMU0_PLAGO Unreviewed; 999 AA.
AC A0A1Y1JMU0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000256|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=PGO_130670 {ECO:0000313|EMBL:GAW82795.1};
OS Plasmodium gonderi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW82795.1, ECO:0000313|Proteomes:UP000195521};
RN [1] {ECO:0000313|Proteomes:UP000195521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521};
RA Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.;
RT "Plasmodium gonderi genome.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
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:GAW82795.1}.
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DR EMBL; BDQF01000014; GAW82795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1JMU0; -.
DR EnsemblProtists; GAW82795; GAW82795; PGO_130670.
DR OMA; FRCGLIK; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000195521; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR Pfam; PF05470; eIF-3c_N; 2.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000195521}.
FT DOMAIN 743..915
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 116154 MW; 194FA8B02CA23E82 CRC64;
MQSKFWAKGV DDESGDNVTE SSDNEIDDKK PLVPAQAERW AAIDSSSSEE EERVIKSYEG
KRLDFYKNIG SSLNESMESN DFNQLLKDYE NLYKFMIKES PERIPNFAIV YLDKFTKYVE
TTFQSNVEKK DLSKNKAQTL NKLRAKIRKC SEFYQNKLNL YHENPDDFKA ALEDELDEDE
DEEEEDDEEE EEDDEQEEEG AGGIVKDNED DSIKDAEGKK KKKKEKENDE KSGQDDDSSD
DWSYSDGDEY ASDDADDKTK SAMSKWGLKT SEKVEKKKVV KTKKVKKEGT KKEEKTAQVD
ENQSAKNKAY AELLSTKNLS EEVIRNRVKF VIEKRGRKGL DKHEHINILS KLSELAKTIS
TQSYIEVLEQ LINLEFDIVS SVYTYMSFNI WNKAFKYIEL ILDILIQNES FYLVSINITE
EITEEIITEK EKISRSCKTL ISFLAKLDDE LLKALLYIDA QTEEYRKRLG KTVHMIALLY
KGYNYVKFTK KLPDLAIYIS MRILEHMYYK PEALFMQIWN FVTSRKENNT SLTDADRTNG
GRKETDMENN GSGNANVFSS LNGGSNVNGS IKENGDLKAC YNTQTNGDMD KQLNEQSPKQ
ADKLGSKIDD NNMSPKKVVE KYVYEIFEYG TKQQKIKALL QLSFNRSLQD EFLEAKELLN
VANVHELALS SDIQTQILYN RNLIQLGLCA FRHGRIYEAH CCLGEICSQN KHRELIAQGV
STLKNQEKTL EQERAEKRRL LSFHMHISIE LIECVNNICA MLLEVPNLAR HTYESKKDII
SRQFRRFLDI YDKQVFNNPP ENNKEIILLA TKYLQKGNWK LCCEKIFSLS VWSKFSDRER
VQNILQERIK QEAMRTYIFR YISIYDSFAV DQLCIMFDLS ENSVHSILSK MMINHEIPAC
WNESSKHIII NKVNPTALQT VAIKLAENIN EVMEQNELAF NMRNPKFMFM QEKRTQMKDD
KSSWLHKKGD GKYGKSYHQH KNVHYKKNFK EKIVSKNFA
//
