GenomeNet

Database: UniProt
Entry: C1MVZ0_MICPC
LinkDB: C1MVZ0_MICPC
Original site: C1MVZ0_MICPC 
ID   C1MVZ0_MICPC            Unreviewed;       996 AA.
AC   C1MVZ0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
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};
DE   AltName: Full=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03002};
GN   ORFNames=MICPUCDRAFT_59561 {ECO:0000313|EMBL:EEH55787.1};
OS   Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN   [1] {ECO:0000313|EMBL:EEH55787.1, ECO:0000313|Proteomes:UP000001876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH55787.1,
RC   ECO:0000313|Proteomes:UP000001876};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG663741; EEH55787.1; -; Genomic_DNA.
DR   RefSeq; XP_003059835.1; XM_003059789.1.
DR   AlphaFoldDB; C1MVZ0; -.
DR   STRING; 564608.C1MVZ0; -.
DR   GeneID; 9685274; -.
DR   KEGG; mpp:MICPUCDRAFT_59561; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   OMA; FRCGLIK; -.
DR   OrthoDB; 5482362at2759; -.
DR   Proteomes; UP000001876; 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:UP000001876}.
FT   DOMAIN          668..840
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..218
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..946
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..985
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  109708 MW;  CA5944F767C787A2 CRC64;
     MASKFWGGDS SDSGSDSGSE SSSSSSNGSG SSSSGSSSSG SSSSSESDAG PSKYLQAGSS
     DSSSDEGVRV VRSAKDKRFI EARAIADEMR NKIKNNDWIS LQTLFDKLNK QLERVMRLQN
     EVGGGVPKFY YRALATLEDA IEATFANKPA IKKMSSTNAK AFNAMRQRLK KHQRDDPTVE
     AGIRAAHEKM ESTDEDESEP ESDSDSDADD DDDEKENKQS ADADDGFETV GKGGKTKGKG
     AAAAAAAQPP KELDVMTAPK EKITYEMVDK KLKDIIASRG KKGTDRHENA ENLAYLATVS
     TCASQEIESL IMLISAQFDI SGSMSAHMPI PIWKRCVNNL LRIDKLLSEN KQITLTEDVE
     PQPKPPPEDI VAGAPVQLWG SLCAFTERLD DEYFKSMQSI DPHSKEYLFR MQDESLFIVL
     CAAVVRYYEN RDDATEIHCK LSLRLLEHLY YKPEPVYEAL RKFATAKLED ADALEAKLAA
     DAVAAAAAAK AKEEAKRIRD KQAEEEDEEY LDDEDADQAE AKEAQEIPYP AGFRFPAPSL
     PETLKKLSLT IYKDGDTRSK ARAMLCEIFQ KGLVGDFRAG RDLMLMSHLQ ENISHMDIST
     QILFNRAMAQ LGLAAFRGGL FAEAQSCLGE MYQGGRVREL LAQGVTQSRF HERSIEQEKL
     ERRRQMPFHM HINLELLESV HLVTSTLAEV PYMTQTSTRR ARSTNKPFTR ICDNYERQTF
     NGPPENVRDN VMAAVRFLLD GRWSHAKDII LGLEAWKLLP GDAAPVLEKV VNRLKEEAMR
     TYLFQFAAQY NSVSMDVIGN MFDLDQKSAH SIVSRMIINE ELRGMCDAVT NSVVMSHAEP
     TRLQSLAMTF AEKCAVLLDA NERALELHVG TGGAQLFDYD DDGGGDGGRR GGRGGRGGRG
     GRGAGGEWED DGGGGRGGRG RGGRGGRGGG RGRGDRDGRD GGGRRRQESY SNFSTRRGAE
     GDFAKRGGGK FKKDPKEDQR DPTERMVSLK AGNWRR
//
DBGET integrated database retrieval system