ID A0A395T0G2_9HYPO Unreviewed; 860 AA.
AC A0A395T0G2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=FLONG3_4025 {ECO:0000313|EMBL:RGP77849.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP77849.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP77849.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP77849.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP77849.1}.
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DR EMBL; PXOG01000083; RGP77849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395T0G2; -.
DR STRING; 694270.A0A395T0G2; -.
DR Proteomes; UP000266234; 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 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:UP000266234}.
FT DOMAIN 601..775
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..191
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 96796 MW; 71EFD03005DD732E CRC64;
MSRFFRGGDD SSSDSSSEEE DLYSEEEEEE EQQQDSQEES SDVNDSDDSD SDDEGGKGIN
KFLKDASSDS DDSDDEVRAK VKSAKDKRLD ELESSIKQIE NGQKNGDWTL ISGEYEKLNR
QVAKLPGSRP PKSYIRILAE LEDFMNESLA KQKVTPKKMN AIQARSLNAV KQKVKKTNKE
YQSQIDAYRA DKDAFMDSSD NEPVVAAPKP KAKTVSLQVD AAPTEEGDDG FATVGKGGRT
LQYTPESIFK HLRTIMESRG KKNTDRTEQI KTMEKLNEIA NTPYQKIRVL LTLVSTRFDV
GSGGASAMSV EHWKAAEKEL SSLLQVLEEN HDYVVVENAE EWDDDEKPPA LQEGEKHIKV
PGSIVSYIER LDDELVRSLQ SIDPHTSEYI ERLQDEGALY NIIFRGGLYY EYLRKDDSLE
IPQDSVNRIV MRRLEHVYFK PAQVVQTFEE NCWKTVGDSI ESVITPRDQA QNAGNLVNVL
CNYLFSHSEG IIRARAMLCQ IYFLALHGEY YRARDMMLMS HLQENIPNFD VQSQILYNRT
LVQVGLCAFR KGLVYEAQNT LQEICGSGRQ KELLAQGVMM QRYNQVSPEQ ERLEKQRQLP
FHMHINLELL ECVYLTCSML LEIPLLAQTG SSPDVKKRVI SKTYRRMLEY HERQIFTGPP
ENTRDHVMQA SKALAAGEWK KSIEFIHSIK IWELMPGAEE IKTMLSKQIQ EEGLRTYLFT
YAPFYDTLSI ETLSAMFELD TAKVAAVISK MISHEELAAS LDQVTSTVIF RKGVELSRLQ
SLALALSDKA SALIESNERT LEQKTQGTSN AFERQGGRGR GGQRRGGGQG RGGARAGGNT
QRQAGGTQFT GGALGAAVRG
//
