ID A0A1W5CXG2_9LECA Unreviewed; 859 AA.
AC A0A1W5CXG2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=FRX48_03490 {ECO:0000313|EMBL:KAA6412499.1};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM35470.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SLM35470.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAA6412499.1, ECO:0000313|Proteomes:UP000324767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1-1 {ECO:0000313|EMBL:KAA6412499.1};
RA Greshake Tzovaras B., Segers F., Bicker A., Dal Grande F., Otte J.,
RA Hankeln T., Schmitt I., Ebersberger I.;
RT "The hologenome of the rock-dwelling lichen Lasallia pustulata.";
RL Submitted (SEP-2019) 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; VXIT01000005; KAA6412499.1; -; Genomic_DNA.
DR EMBL; FWEW01000731; SLM35470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5CXG2; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000192927; Unassembled WGS sequence.
DR Proteomes; UP000324767; 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}.
FT DOMAIN 601..775
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..194
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 96977 MW; 1ADD523A373EC843 CRC64;
MSRFFTAGDS TSESSSSDEE ELYSDHEAEE KSDEESSSEE EEGSDEDGSS SSDDEGGKRG
VTKFLKDQVS SDESEDEDKV TIVKSAKDKR LEELDGIVKL IENALKINDW SSISTEFDRL
NRQVTKMSGL EKIPKNYVRT IADLEDFMNE AIAKQKVSTK KMNATNAKGL NAMKQKIKRN
NREYTAEIDK YREDKFEYLI SDEEEVVTVE KTKKPKTAYV DGIDGGDDEG FSTVGRGGKT
LQYTPESIFK HLRSIIESRG KKNTDRTEQI RVMEKLLEVA TTPYQRIRVL LTLISTRFDL
TSGSAATFMS QEQWKMAEHE FGTLLEVLEE NHDIVVLENA EEWEDDEKPP QPTPGEKLRI
PGSIVSIVER LDDELTRSLQ HIDPHTAEYI ERLSDEQALY TNIVRGLLYV ENLKKDVKLE
VPQDNANRVI MRRLEHIYFK PSQVVNILEE TTWKAIPSEL ESNITPRGKI SDTAALVQTL
CSYLFEQSDG IIRARAYLCQ VYFLALHDQY YRARDMLLMS HLQETIGNFN INTQILFNRT
LVQVGLCAFR VGLVYEAQNT LQDICGSGRQ KELLAQSIMT QRYSQVSPEQ ERLERQRLLP
FHMHINLELL ECVYLTCSML LEIPLLAQTG SSPDIKKRII SKTYRRLLEF HERQIFTGPP
ENTRDHVMQA SKALAAGEWK RAAELINSIK IWDLMAQPDK IKAMLAEQIQ EEGLRTYLFT
YAPFYDTLAV GTLSSMFELP ERMVAAVVSK MISHEELAAA LDQVNSAIIF RKGVELSRLQ
SLALTLSDKA SGLIEANERT LEQRTQGTAN AFERQSGPGG RGGRGGRGGR GGQRGARTGE
RTRGGQQFGG GALGSAIKA
//
