ID A0A1Z5TP68_HORWE Unreviewed; 859 AA.
AC A0A1Z5TP68;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=BTJ68_02474 {ECO:0000313|EMBL:OTA37711.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA37711.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA37711.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA37711.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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}.
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:OTA37711.1}.
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DR EMBL; MUNK01000017; OTA37711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TP68; -.
DR STRING; 1157616.A0A1Z5TP68; -.
DR VEuPathDB; FungiDB:BTJ68_02474; -.
DR InParanoid; A0A1Z5TP68; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000194280; 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:UP000194280}.
FT DOMAIN 603..777
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 97105 MW; EB13227ABDB5C891 CRC64;
MSRFFHGDSS SESSSEEEEE LYADEQEEES SEEESSEEES EEGDEDSDSD SSGDEAGKTG
ASRFLREVSD DSDESDEEKV TVVKSAKDKR FDELEGTIRL IENAEKISDW NAINEQYDRM
NRQLPTLQRD LEGKPPKMYV KTVAELETAV SEAFEKQKVT PKKMNPIAQK GLNALRQKIR
KNNRDFQGDI EAFRKNPDEF MKEDVVEDTA PAPKKPKKKL VENQNDVDAN DEGFTMVGAG
GKAMVYTAES ILKHLRQIVE SRGRKNTDRL EQIRIMEKLL DVAHTDYQRI RVYLTLIATR
FDLTSGTGSQ MSQEQWKLAQ QEIGALLGIL EQNHDLVVVE GAEEWEDDEK LPTVEEGSVF
KIPGSVVSFV ERLDDELTRV LQQVDPHTAE YVERLADEGT LYTNILRCMC YAERLIVQEK
VTAPQENVNR VVMRRLEHLY FKPSQVVNIL EENVWKALPK ELDSKITPRS QSSDVTKLVQ
TLSGYLFNKS EGIIRGRAML CQIYHLALHD HYYKARDMML MSHLQETIQS FDVNTQILYN
RTLTQVGLCA FRAGLVYECQ TALQDICGSQ RQKELLAQGL QIQRYSQITP EQERLERQRQ
LPFHMHINLE LLECVYLTCS MLLEIPTLAQ SGSSPDLKKR VISKSYRRML EYHERQIFTG
PPENTRDHVM QASKALAAGE WKKAADFITT IKIWDLLPKN AEIKQMLEQQ IQEEGVRTYL
FTYAPFYDTL AISHLAGMFD LPESKVTALV SKMIHHEELA AALDQVNSAI IFRKGVELSR
LQSLALTMSD KASGLIEANE RTLEQRTAGS ANAFERQGGQ RGRGGARGRG GRGGAFGGRG
GGRGGGFTGG ALGNAIRAQ
//
