EIF3C_ASPFC
ID EIF3C_ASPFC Reviewed; 862 AA.
AC B0YEH1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 93 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
DE Short=eIF3 p93 {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=Translation initiation factor eIF3, p93 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
GN Name=nip1; ORFNames=AFUB_099160;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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:0000255|HAMAP-Rule:MF_03002}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|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; DS499603; EDP47315.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YEH1; -.
DR SMR; B0YEH1; -.
DR EnsemblFungi; EDP47315; EDP47315; AFUB_099160.
DR VEuPathDB; FungiDB:AFUB_099160; -.
DR HOGENOM; CLU_004304_0_2_1; -.
DR PhylomeDB; B0YEH1; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
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:EnsemblFungi.
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; 2.
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 Cytoplasm; Initiation factor; Protein biosynthesis.
FT CHAIN 1..862
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000364274"
FT DOMAIN 600..774
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 97509 MW; C8C9160DD0D026ED CRC64;
MSSRFFYGGG SDSDSSSSDE EELYSDREEE EKSEEEESSE EEDETSEEEE SDEETGARKF
LKDVASDSEE EEEEEKVTVV KSAKDKRLDE LENTIKLIEN AKKINDWAVI STEFDKLNRQ
VAKITQSGPT PKIYIKAVAD LEDFVNETVA KQKSGDKKLN ASQAKGFNAA KQRIKKNNKD
YGNLIDKYRK DKEDFMESDD EEAIPVIAAP RITKLERIEA PAAAIDDDGF ATVGRGGKTL
QYTPESILKH LRVIVESRGK KNTDRMEQIR TMEKLLEVAQ TPYQRIRVYL TLISTRFDLT
STSSANYMAV DQWKSAEQDF SSLLSVLENN RDHVVFEGAE EWEDDEKQPT IAPGETLYIP
GSIVSFAERL DDELTRSLQH IDPHTAEYIE RLSDEKLLYT DLVRAQAYVE GLNEVEKTDP
RQDSVNRVVM RRLEHVYFKP SQVITILEDA TWKSLPSELD SSITPRASSG NVENLVLSLC
NYLFKYSDGI IRARAMLCQI YFLALHDQYY RSRDLMLMSH LTENISNFDV STQILFNRTL
VQIGLCAFRS GLIYEAQNTL SEVCGSGRQK ELLAQGIIMQ RYSTVSPEQE RLERQRQLPF
HMHINLELLE CIYLTSSMFL EVPLMAQTSS SPEMKRRVIS KTFRRMLDYN ERQVFTGPPE
NTRDGVIMSA KFLAAGDWKK AAEMLNSIKI WDLMPQPDKI KEMLSQQIQE EGLRTYLFTY
APFYDSLSIA TLSNMFELSE KKISAIISRM ISHEELAAAL DQVNNAIVFR KGVELSRLQS
QIVTLADKSM NLLEANEKTL EQRTQGMANA FQRDQGAGAR GGRGSGRGGQ ARGGPRFPGG
QQGRRPGGQQ FGGGALGGAI KA
