EIF3C_NEOFI
ID EIF3C_NEOFI Reviewed; 862 AA.
AC A1D9P1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=NFIA_029540;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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}.
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DR EMBL; DS027693; EAW20522.1; -; Genomic_DNA.
DR RefSeq; XP_001262419.1; XM_001262418.1.
DR AlphaFoldDB; A1D9P1; -.
DR SMR; A1D9P1; -.
DR STRING; 36630.CADNFIAP00002714; -.
DR EnsemblFungi; EAW20522; EAW20522; NFIA_029540.
DR GeneID; 4589122; -.
DR KEGG; nfi:NFIA_029540; -.
DR VEuPathDB; FungiDB:NFIA_029540; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_2_1; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR Proteomes; UP000006702; 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; Reference proteome.
FT CHAIN 1..862
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000364286"
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; 97381 MW; AC5F2C4FC974C7C8 CRC64;
MSSRFFYGGG SDSDSSSSDE EELYSDREEE EKSEEEESSE EEDETSEEEE SDEETGAKKF
LKDVASDSEE EEEEEKVTVV KSAKDKRLDE LENTIKLIEN AKKINDWAVI STEFDKLNRQ
VAKITQSGPT PKIYIKTVAD LEDFVNETVA KQKSGDKKLN ASQAKGFNAA KQRIKKNNKD
YANLINKYRK DKEDFMESDD EEATPVIAAP RITKLERIEA PAAAIDDDGF ATVGRGGKTL
QYTPESILKH LRVIVESRGK KNTDRMEQIR TMEKLLEVAQ TPYQRIRVYL TLISTRFDLT
STSSANYMAV DQWKSAEQDF SSLLSVLENN RDHVVSEGAE EWEDDEKQPT IAPGETLYIP
GSIVSFAERL DDELTRSLQH IDPHTAEYIE RLSDEKLLYT DLVRAQAYVE GLNEAEKTDP
RQDSVNRVVM RRLEHVYFKP SQVITILEDA TWKALPSELD SSITPRASSG NVENLVLSLC
NYLFKYSDGI IRARAMLCQI YFLALHDQYY RSRDLMLMSH LTENISNFDV STQILFNRTL
VQIGLCAFRS GLIYEAQNTL SEVCGSGRQK ELLAQGIIMQ RYSTVSPEQE RLERQRQLPF
HMHINLELLE CIYLTSSMFL EVPLMAQTSS SPEMKRRVIS KTFRRMLDYN ERQVFTGPAE
NTRDGVIMSA KFLAAGDWKK AAEMLNSIKI WDLMPQPDKI KEMLSQQIQE EGLRTYLFTY
APFYDSLSIA TLSNMFELSE KKISAIISRM ISHEELAAAL DQVNNAIVFR KGVELSRLQS
QIVTLADKSM NLLEANEKTL EQRTQGMANA FQRDQGAGAR GGRGSGRGGQ ARGGPRFPGG
QQGRRPGGQQ FGGGALGGAI KA
