ID K0L085_WICCF Unreviewed; 861 AA.
AC K0L085;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=BN7_6417 {ECO:0000313|EMBL:CCH46818.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH46818.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH46818.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
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:CCH46818.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAIF01000274; CCH46818.1; -; Genomic_DNA.
DR AlphaFoldDB; K0L085; -.
DR STRING; 1206466.K0L085; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_2_1; -.
DR InParanoid; K0L085; -.
DR Proteomes; UP000009328; 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:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:UniProt.
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 GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProt.
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; 2.
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:UP000009328}.
FT DOMAIN 592..766
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 97023 MW; 1DA732FEF05851E8 CRC64;
MSRFFAGGVS DSDYSSSEEE LLSSSEEEEE LRSESEDEEA EESDDSAFAN DSDDSDSDED
TPSGPAYFLK SKFTKGAASD DDSSDEEDGK KVVKSAKDKL LDEIRSAINT IDTSKEDNDW
IVVLSEFDKL NRLLIRAQQQ NLSTPNIYIK TIAQLDETIQ DTQQDKKKLN ASVSKAFNTV
RQRVKKAVRE NSSLVDSFRE NPEAFEKEAP ITETPSKAST PVPGEGFSTV GKSGKTTEST
SFFKTLRSVA ESRGKKNVDS REQVKTLETL AEEASTPYQA IIVYLMLIPY RFDGSANLSY
LSIDQWKLAA KDINNLFKIL EDNKSQYRVT ETAEASDDIE VEPTPNSEGV REVVGSVVSF
VERLDDEFTR SLQVIDPHTT EYIDRLKDEQ ELYTTIIRAQ LYSEFIIPES EIVSAKGDQI
ARVVSRRIDH IYFKPSGLIK QSEATAWESL KPTAQTSYIA PYTEEESYID TLLDSLASIL
YRQTNAVYRK RAMLSHIYFY AFNNKYFKAR DMFLISHLQS SIHTSDPSVQ ILFNRALVQL
GLCAFRNGLI SEAHQTLQEI ATSTRHKELL GQGAQRYSNQ NTVADKQRLL PFHTHINLEL
LETVFLTSSL LIEIPQYAQL GTSVDAKKRL QTKSFRRTLE YHEKQTFQGP PENTRDYVMT
AAKQLQAGNW KKASELLNSI KIWNLFPESD KIRELIKEKL QVEGLRTYIF QFKSFYSKLS
IVKLSQIFEL SESKVSAVLS KMIFNEEISA GLDQVSKSVV FTKGVELTRL QELALDLADR
ASSLSDRNER LAGGHQQQQG YHHGGNNAGK DQHNNAHHHK RNQNFKFAPV TGALSSAPGS
ISGALNGMDK RNNQRGKSTR A
//
