ID M2XK90_GALSU Unreviewed; 956 AA.
AC M2XK90;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=Gasu_22270 {ECO:0000313|EMBL:EME30557.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30557.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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; KB454499; EME30557.1; -; Genomic_DNA.
DR RefSeq; XP_005707077.1; XM_005707020.1.
DR AlphaFoldDB; M2XK90; -.
DR STRING; 130081.M2XK90; -.
DR EnsemblPlants; EME30557; EME30557; Gasu_22270.
DR GeneID; 17089279; -.
DR Gramene; EME30557; EME30557; Gasu_22270.
DR KEGG; gsl:Gasu_22270; -.
DR eggNOG; KOG1076; Eukaryota.
DR OMA; FRCGLIK; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000030680; 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; 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:UP000030680}.
FT DOMAIN 704..884
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 109408 MW; ADABB37CD6F99343 CRC64;
MTSRFFATGD TSSSESERSE HTEDSYVSGD ESSEAESNDG NKATGFEVGE RLARYLRDSD
SEEGEEKRVV RSARTKQQEA LLSIIQQLKN HIKISDWISI QSDFDALNRQ LQKFYKVDVL
SESRKEPPKA YISAIVLLED FLNKTAENKD KKLSKTNTKA FNAVKQRLKK NNREWEEYIR
KFRESGAIPG EDLHDEDEGT GEGVDEEQEE SEANESWDDS EAESLGDSEQ AKPATSGGSQ
WLLKTSGLSK GSQATSHKER KKSKSQILQQ SGQSFKETFD NIPAIASKDF GITEDLSESA
IDQKLVEIIA TRGRKGTSKR ESLLQLEMLL KVAKTLVQEM EILFQIVSTH FDMTPLSIGY
MSQENWRNCV QCIEKILNLA FEHETQVRFV VNHPSTETLD VSVPIRGDKT TSQIEESIES
ETNGDKNDKR KCVRGDIATL LERMDDDLFR AWQGIDAYLP EYVDRLKDEF VLLKLLAKAQ
TYFEKEEELD RAARIACRRI QHLYYKPDDL IVGMIQASLQ KTRKQLQVIH DEDPVLSGLV
YLNETQDESL LLDIPELPIH QRPLKGEQAL LRLAVLVYRY GSENLKSIVI LCQIYHHALE
NRYYEARDML LMSHLQESIG LLELPLQILF NRTMAQLGLC AFRHGLAQET LYCLQELCTP
VHTGLGSSTV ARLKELLAQG IVQQRGHEKT LEQERLERNY QIPYHMYLPV DFIEMAHLIA
AMVIEIPSLT RAEAKNEAPQ KRKIYSRVFQ HFLRNSIRQA YPSPPENTRD YIMSASRAFL
YRFTLEICLS TDIASIRAWE SIDVASAQSI LQTWRNLIQV EGLRTFIHSY ASYFDSLSVA
FLSEWFELSP ARVHSLISKM IMNEELQASW DQPSGCVLIK RWEPNHLQSL CLQLTEKCSQ
LIDYNERLLD ARSGGQMLKT EEREEFLKTA SHWMNAGGNR KLSTTENWVK SRTAAS
//
