EIF3C_ASPCL
ID EIF3C_ASPCL Reviewed; 862 AA.
AC A1C987;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=ACLA_054580;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027048; EAW13411.1; -; Genomic_DNA.
DR RefSeq; XP_001274837.1; XM_001274836.1.
DR AlphaFoldDB; A1C987; -.
DR SMR; A1C987; -.
DR STRING; 5057.CADACLAP00005162; -.
DR EnsemblFungi; EAW13411; EAW13411; ACLA_054580.
DR GeneID; 4707059; -.
DR KEGG; act:ACLA_054580; -.
DR VEuPathDB; FungiDB:ACLA_054580; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_2_1; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR Proteomes; UP000006701; 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; 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 Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..862
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000364273"
FT DOMAIN 601..775
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 814..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 96814 MW; 1003FC1F21E855C4 CRC64;
MSRFFYGGGS DSESSSSDEE ELYERDEEEQ SEEEESSEEE ETSEEGSDDE EGGVTGAARF
MRDMSESEES EDEEKTTVVK SAKDKRLEEL ESTMKLIDNA KKINDWAVIS TEFDKLNRQI
VKITQAGPTP RVYIKGVADL EDFVNETVSK QKSGDKKLNA SNAKGFNAVK QRIKKNNKDY
ANLIDKYRKN KEAFLEGKDE AAAPAAAAPR VAKLERVEAP VDVPVADDEG FATVGRGGKT
LQYTPESILK HLRVIVESRG KKNTDRLEQI RTMEKLLEVA QNPYQRIRVY LTLISTRFDL
TSTSSANYMA PEMWKSAEQD FSSLLSVLEN NRDYVVTEGV DEWEDDEKQP QVAAGETLYI
PGSVVSYAER LDDELTRSLQ HIDPHTAEYI ERLSDEKQLY TSLVRAQAYV EGLSKAEKSD
PKQDSVNRVV MRRLEHVYFK PSQVITILED ATWKALPSEL DSGVTPRGKT GDVENLVLTL
CNYLFQYSDG IIRARAMLCQ IYFLALHDQY YRARDLMLMS HLTENISNFD VSTQILFNRT
LVQIGLCAFR AGLIYEAQNT LSEVCGSGRQ KELLAQGIIL QRYSTVSPEQ ERLERQRQLP
FHMHINLELL ECIYLTSSMF LEVPLMAQTS SSPELKRRVI SKTFRRMLDY NERQVFTGPA
ENTRDGVIMS AKFLAAGDWK KAAEMLNSIK IWELMPQPEK IKEMLSQQIQ EEGLRTYLFT
YAPFYDSVSV ATLASMFELS EKKISAIISR MISHEELAAA LDQVNGAIVF RKGVELSRLQ
SQIVTLADKS MALLEGNEKT LEQRTQGMAN AFQRDQGAGA RGGRGGGRGG HARGGARFPG
QQGRRPGGQQ FGGGALGGAI KA
