ID A0A0E9NCJ5_SAICN Unreviewed; 1241 AA.
AC A0A0E9NCJ5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=G7K_1764-t1 {ECO:0000313|EMBL:GAO47559.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO47559.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO47559.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO47559.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO47559.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO47559.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO47559.1}.
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DR EMBL; BACD03000009; GAO47559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NCJ5; -.
DR STRING; 698492.A0A0E9NCJ5; -.
DR OMA; NIDSRYL; -.
DR Proteomes; UP000033140; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; 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 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:UP000033140}.
FT DOMAIN 986..1160
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 346..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..443
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 139586 MW; 3CA7A3DEA4A79C28 CRC64;
MLLGDGRRHG DAVIMICTFR DVDGRLRPFC ERSCVCEDEP TQCLSGADID PVPTRTVKVA
SSFTYALTLL DFEQRPVNRD IPKSSGIFRV LRTIVFLLLL SDHWTVQALI VRQILPTYNE
QRLVLRSVTS WELAAMSFYG DEKIYLRGTR VGTSPLSTSD EPAVGGRDRG HLSKIDLVHE
SGKAFKNKAY GARHGVKTAY AVASSVRGKR LHEEGVDMSA ISQKKVRVWV FIPDEQPSPR
FTNAFVTETV RGVHQGFGKI IQPILHTSHL RPAPADTLEV DLCTGRLIRY IQMTENVAYN
YYKRILDISC EPLIPFYSSL KCLPVLCPVL KNFETEAPKE HVCRQLSVRS SHSVKPPSLN
AQSSRVTAVV VRTINSSQRI SQQSTMSRFF RASSDTESSS DESEVDISTS ESGSSEASGS
ESESDSEESS DDSDNDSSDD DSSSDEDGPS RGANRFLKGG DSDDSDEEEE TKRVVKSAKD
KRYDEIVSSV SVIANATKIN DWVTISTEFD KLNKLTQKTK QLDGRIPRVY IKAIGKLEDA
LNESVKNEKQ SKKKMNASNA RALNSLKQRI RKNNRDFESE IAQWRANPES FENEDEPEPA
AAPAAKAQRK VEEDVEVDGK ADGDDGFSTV GKKGRTEKVT AEDIFKQLRA VVEARGKKNT
DRNEQISILE KLVDVAITPY QKLRIFLALI SARFDATPST ALYMASEQWE AASKDLSKLF
ELLEEQPKFM VAEDADDLED EDVQVPEGDE VVRVRGSVIA YVDRLDDELT KALQHIDPHT
SDYVERMKHE AGLYYIIVRS HCYFERVKLA DSIAAAVARR LEHVYFKPEQ VVAILEENTW
KNLPQGINSS VTPREAAVNV TDLVQTLCVY LYKNGQSLHR TRAMLCHIYH HALHNRYHQA
RDLLLMSHLQ ESIHQADIAT QILHNRTMVQ LGLCAFRAGM VNEAQQCLQE ICSTGRIKEL
LAQGVQRYNQ VSPEQERMDR QRQLPFHMHI NLELLECVYL TCSMLLEIPA MAAAGSSPDA
KKRVISRPFR RMLDFNERQV FVGPPENTRD HIMQAAKALA AGEWQKAREL ISAIKIWDLM
PNTEEIKTML GEKIQEEGLR TYLFTYASFY ETMSIASLSE MFDLSERSVT ALVSRMISHE
EIPAAFDQVS SAIIFQRVEP SRLQALAIGF ADKANHFVEA NERLLESKTQ TEGERRQGQD
GRDRRQRDGP RNNQTGGRVG GGNRGRGRNN FNSAIGRSVR A
//
