ID A0A1D3TM01_9APIC Unreviewed; 970 AA.
AC A0A1D3TM01;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 Name=EIF3C {ECO:0000313|EMBL:SCP05989.1};
GN ORFNames=POCGH01_13016100 {ECO:0000313|EMBL:SCP05989.1};
OS Plasmodium ovale (malaria parasite P. ovale).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=36330 {ECO:0000313|EMBL:SCP05989.1, ECO:0000313|Proteomes:UP000242942};
RN [1] {ECO:0000313|EMBL:SCP05989.1, ECO:0000313|Proteomes:UP000242942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PocGH01 {ECO:0000313|EMBL:SCP05989.1};
RG Pathogen Informatics;
RL Submitted (JUN-2016) 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}.
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DR EMBL; LT594594; SCP05989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3TM01; -.
DR VEuPathDB; PlasmoDB:PocGH01_13016100; -.
DR VEuPathDB; PlasmoDB:POWCR01_130012700; -.
DR Proteomes; UP000242942; Chromosome 13.
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; 1.
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:UP000242942}.
FT DOMAIN 713..885
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 165..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 112550 MW; 283FC73D3F8A97FA CRC64;
MQSKFWAKGV DDDSGDNVTE SSESEVDEKK PLVSAQAERW AAIDSSSSDD EDRVIKSYEG
KRLDFYKNTG NSLNEGMENN DFIQLLKDYE NLHKFMIKES SERIPNFAIV YLDKLTKYVD
STFQNNVEKK NLSKNKAQTL NKLRAKIRKC SEFYQTKLKL YHENPDDFEV DLGKEDEDEE
DEEEEEEQDN ADDVDDVDDA DDADDADDNR KKDGGKKGDG DESDDWSYSE DEEYASDEED
DKTKKAMSKW GLKTSDKVEK KKVVKEKKVK KEGIKKEEKN VQLDENQSAK SKAYAELLNT
KNLSEEVIRN RVKLVIEKRG RKGLDKHEHI HILSKLCEIA KTISTQSYME VLEHLINLEF
DVVSSVYTYM SFSIWNKTFR YIELILDLLI QNDNFSLLSS NITEEIVTEV LNEKEKTSRS
CKTLISFLAK IDDELLKALI YIDAQTEEYR KRLGKTVHVI GLLYKGYNYV KYAKKMPDLA
IYISTRILDH LYYKPEPLFR QIWNFLNSEK ETLQQENITG EANTGVSNGK INAESNGQIS
TQSNGHTNAL CNGQITKDNK NASGGGDDEK STKASPLNMI KEECPQKIVE KYVYEIFEYG
TKQQKIRALL QLSYNKSLYD DFLHAKELLN VANVHELALS SDIQTQILYN RNLIQLGLCA
FRHGKIYEAH CCLVEICAQN KHRELIAQGI STLKNQEKTV EQERAEKRRL LSFHMHIPIE
VIECVNNICA MLLEVPNLAK HSYESKKDII SRQFRRFLDI YDKQIFNSPP ESNKEIIILA
TKHLQKGNWK SCCEKIFSLS VWSKFPDREK VQSILEQRIK QEALRTYIFR YISIYDSFSV
DQLCIMFDLS HNAVHSILSK MMINHEIPAC WNESSKFIII KKVHFTSLQS VAIKMAENIN
DVMEHNELTL NMRNPKFMFM QERRTQMKDE KSGWSNKKGD SKYGKGYGHH KNTQYKKNFK
DKTIKNYVQN
//
