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EIF3C_EMENI
ID   EIF3C_EMENI             Reviewed;         860 AA.
AC   Q5AX75; C8VDC8;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=AN7105;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(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: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; AACD01000119; EAA61310.1; -; Genomic_DNA.
DR   EMBL; BN001304; CBF79072.1; -; Genomic_DNA.
DR   RefSeq; XP_664709.1; XM_659617.1.
DR   AlphaFoldDB; Q5AX75; -.
DR   SMR; Q5AX75; -.
DR   STRING; 162425.CADANIAP00000360; -.
DR   EnsemblFungi; CBF79072; CBF79072; ANIA_07105.
DR   EnsemblFungi; EAA61310; EAA61310; AN7105.2.
DR   GeneID; 2869818; -.
DR   KEGG; ani:AN7105.2; -.
DR   VEuPathDB; FungiDB:AN7105; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; Q5AX75; -.
DR   OMA; VVMHRSE; -.
DR   OrthoDB; 273138at2759; -.
DR   Proteomes; UP000000560; Chromosome IV.
DR   Proteomes; UP000005890; 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:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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..860
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000364283"
FT   DOMAIN          599..773
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..50
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  97178 MW;  AABF2A886596BD36 CRC64;
     MSRFFYGNDS DSDSSGSDEE ELYSDEEVEQ SEEESSEEDA SSEEESSEDE DAGKAGASRF
     MKDVSDSEES EEEDVVKVVK SAKNKRLEEL ESTIKLIDNA QKINDWAVIS SEFDKMNRQV
     VKVLQSGPVP KIYVKTVADL EDFVNETVAK QKSSNKKMNA SNAKGFNAIK QKIKKNNKEY
     AAQIEKYRAD KDSYMESDEE EEKKPAIAAP RLSKLERVEA PVAVAGDDDG FETVVRGKTL
     QYTPESILKH LRVIVESRGK KNTDRLEQIK TMEKLLEVAQ TPYQRIRVYL TLISTRFDLS
     TTSTAAYMSV EQWKAAEQEL STLLSVLEKE RNYVVSEGAE EWEDDEKQPQ VAAGETFYIP
     GSIVSYVERL DDELTRSLQH IDPHTAEYIE RLSDEKQLYT NLVRTQIYVE GLTKLEKTEL
     RQDSLNRVVM RRLEHIYFKP SQVITILEEG TDKALPSELE TSITTRGNSD AQTLVQTLCN
     YLFRNSDGIL RARAMLAQIY FLALHDQYYR ARDLMLMSHL SENIANFDVS SQILFNRTLV
     QIGLCAFRAG LIYEAQNTLS EICGSGRQKE LLAQGIILQR YSTVSPEQER LERQRQLPFH
     MHINLELLEC IYLTSSMFLE VPLMAQTSSS PEMKRRVISK TFRRMLDYNE RQVFTGPAEN
     TRDGVIMSAK FLAAGDWKKA AEMLNSIKIW DLMPQPEKIK EMLSQQIQEE GLRTYLFTYA
     PFYDSLSIST LSTMFELSEK KIAAIISRMI SHEELGAALD QVNDAIVFRK GVELSRLQSQ
     IVTLADKSMN LLEANEKTLE QRTQGMANAF QRDQGAGARG GRGPRGGGQA RGGPRLPGGQ
     QRRPGGQQFG GGALGGAIKA
 
 
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