ID F7W101_SORMK Unreviewed; 862 AA. AC F7W101; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 11-DEC-2019, entry version 57. 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 93 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03002}; DE Short=eIF3 p93 {ECO:0000256|HAMAP-Rule:MF_03002}; DE AltName: Full=Translation initiation factor eIF3, p93 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03002}; GN Name=NIP1 {ECO:0000256|HAMAP-Rule:MF_03002}; GN ORFNames=SMAC_02110 {ECO:0000313|EMBL:CCC11453.1}; OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria. OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC11453.1, ECO:0000313|Proteomes:UP000001881}; RN [1] {ECO:0000313|EMBL:CCC11453.1, ECO:0000313|Proteomes:UP000001881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell RC {ECO:0000313|Proteomes:UP000001881}; RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC11453.1}; RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891; RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K., RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S., RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.; RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: RT Sordaria macrospora, a model organism for fungal morphogenesis."; RL PLoS Genet. 6:E1000891-E1000891(2010). 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 ECO:0000256|SAAS:SAAS00891357}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002, CC ECO:0000256|SAAS:SAAS01184759}. CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP- CC Rule:MF_03002, ECO:0000256|SAAS:SAAS01070822}. 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:CCC11453.1}. 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; CABT02000018; CCC11453.1; -; Genomic_DNA. DR RefSeq; XP_003350398.1; XM_003350350.1. DR STRING; 5147.XP_003350398.1; -. DR EnsemblFungi; CCC11453; CCC11453; SMAC_02110. DR GeneID; 10807950; -. DR KEGG; smp:SMAC_02110; -. DR EuPathDB; FungiDB:SMAC_02110; -. DR eggNOG; KOG1076; Eukaryota. DR eggNOG; ENOG410XRU3; LUCA. DR InParanoid; F7W101; -. DR KO; K03252; -. DR OrthoDB; 273138at2759; -. DR Proteomes; UP000001881; 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: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 Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_03002; eIF3c; 1. DR InterPro; IPR027516; EIF3C. DR InterPro; IPR008905; EIF3C_N_dom. DR InterPro; IPR000717; PCI_dom. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR13937; PTHR13937; 1. DR Pfam; PF05470; eIF-3c_N; 1. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50250; PCI; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002, ECO:0000256|SAAS:SAAS01184772}; KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03002, KW ECO:0000256|SAAS:SAAS01070816}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03002, KW ECO:0000256|SAAS:SAAS01070819}; KW Reference proteome {ECO:0000313|Proteomes:UP000001881}. FT DOMAIN 604..778 FT /note="PCI" FT /evidence="ECO:0000259|PROSITE:PS50250" FT REGION 1..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 803..862 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 186..206 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 327..347 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 33..58 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 59..74 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 803..818 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 862 AA; 97511 MW; A28F8DFBFEC82158 CRC64; MSRFFRGGDD SSTDSSSEEE EVYSSEEEEK VKAEDESSSE EESDEEEESE EEEESDSDEE EGPKKKGANR FLQSDDESEE EEEEEQSEDE ATTKVKSAKD KRFDELESTI SQIQNGQKIN DWSLIASEFD KLNRQVVKLQ DGSKAPKSYI KAIADLEDFM NETLAKQKVT PKKMNATNAR GLNAVKQRIR KNNKDYQTQI DAYRKDADAF MESDDEIPAP KTVSKALRFA EAPVVSAEQQ EEDDKGFSTV DSRGKVVQYT PESILKHLRT IIESRGKKNT DRLEQIKVME TLNKVVPITP YQKIRVLQTL ISARFDLGAG GAAQMPLDQW KAAERDLASL LEILEKEKDH VVVEGAEEWD DDDKLPTIPE GEKYLKVPGS VVSLIERLDD ELTRSLQAID PHTSEYIDRL TDEGSLYNTI FRGLLYYEHL RKDASLEVPQ ESLNRIIQRR LDHVYYKPAQ VVKILEENAW KQSGDAGKLI NILSNYLFEN SEGIIRARAM LCQIYFLALH DEYYKSRDLM LTSHLQETIA NFDIATQILY NRTLVQVGLC AFRKGLVYDA QNTLQEICGS GRQKELLAQG VMIQRYSQVT PEQERLEKQR QLPFHMHINL ELLECVYLTC SMLLEIPLLA QTGSSPDVKK RIISKTYRRM LEYHERQIFT GPPENTRDHV MQASKALAAG EWKKATDFIH SIKIWDLMPN TEDIKTMLAK QIQEEGLRTY LFTYAPFYDT LAIATLSSMF ELDSRKVSAV VSKMISHEEL AAALDQVTET VIFRKGVELS RLQSLALTLS DKASSLIETN ERTLEQKTQG SANAFSRKDN RGGGQRGGRG GARGGARTGG NPQRQAGGTQ FTGGALGNAV RG //