ID A0A0C9ZZU8_9AGAM Unreviewed; 873 AA.
AC A0A0C9ZZU8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=PISMIDRAFT_674688 {ECO:0000313|EMBL:KIK27772.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK27772.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK27772.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK27772.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
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DR EMBL; KN833695; KIK27772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9ZZU8; -.
DR STRING; 765257.A0A0C9ZZU8; -.
DR HOGENOM; CLU_004304_0_2_1; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000054018; 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: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:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000054018}.
FT DOMAIN 611..784
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 154..207
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 98775 MW; C80FEA548FE54277 CRC64;
MSRFFRQLGD SDSDTEESDE ELLTSGDEDV PLPKPPQKLS KPTGMSQFLR TAGSDSSSSE
SESSSDDNES DEDDLGGGAK SDEDESDDED VKRTIKSTKD KRLDEIEATG KVMDNALKIN
NWVVISAEFD KLLRLVQRQS NSAEPIPPFF VKTLINLESS LNEAIAKEKE AKKKMNAMNA
RALNSMKQKI KKALKEHEKE TQQYQADPDA FEREFVAHTQ PAETVSARVK KVRQAIVDDG
GDDKPQDDDH FTVVGKGGKA MQFTPDAIFK TLKIVNEARG KKNTDRTEQI RILEKLLEVA
VTSYQRLRVL LALVSSRFDF NTSTTNYMPV ELWLAAQREV DQLISIVALD PSYVVQEHTD
EYDELLERSP ATESDGVVRI RGSIISFVDR LDDEFTKSLQ NIDPHGTEYV DRLKDEKVLY
QTICRAQAYY EHSKQVEPLG RVVMRRLEHI YCKPDAVVGA LESSLTSSDV RPNVVLTPTS
TTSNLIHRLC VHLYKVDNSL LRTRAMLSHV YHHALHNDFY TARDMLLMSH LQESIHSADV
ATQILYNRTV VQLGLCAFRC GLIKEAQATL QDIFATQRVK ELLAQGVHQQ RYQSQLSPEQ
ERAERSRQLP FHMHINTELL EAAFLISSML VEIPLLASIE SEEQKRKVIS KPFRRLLDFA
DRQVFTGPPE STRDHIMQAS KALQDGEWEK CRDLVQNIKI WSLMPEAVSV KEMLANRIQE
QGLRTYLFTY APYYSTLSLS LLSRSFALPL RTVTSIISKM IWNEELSASL DQSTDTVVFH
RIEHSRPQQL AQLISEKINA LVEHNEKTLD SKFGGASGWG DRGDAKGEKR GEQTQERRGN
RTRGALRGTR GRGSKFAQGL GNQMAELSSQ RAH
//
