ID A0A6A4ET19_9STRA Unreviewed; 973 AA.
AC A0A6A4ET19;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 9.
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 subunit 8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=PR003_g15013 {ECO:0000313|EMBL:KAE9331431.1};
OS Phytophthora rubi.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=129364 {ECO:0000313|EMBL:KAE9331431.1, ECO:0000313|Proteomes:UP000434957};
RN [1] {ECO:0000313|EMBL:KAE9331431.1, ECO:0000313|Proteomes:UP000434957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRP333 {ECO:0000313|EMBL:KAE9331431.1,
RC ECO:0000313|Proteomes:UP000434957};
RA Adams T.M., Armitage A.D., Sobczyk M.K., Bates H.J., Dunwell J.M.,
RA Nellist C.F., Harrison R.J.;
RT "Genomic investigation of the strawberry pathogen Phytophthora fragariae
RT indicates pathogenicity is determined by transcriptional variation in three
RT key races.";
RL Submitted (AUG-2018) 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:KAE9331431.1}.
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DR EMBL; QXFT01001018; KAE9331431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A4ET19; -.
DR Proteomes; UP000434957; 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 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:UP000434957}.
FT DOMAIN 709..884
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 109127 MW; 181A081F69DE96F7 CRC64;
MASRFWAGSS SSEEESDVSD VSDVETSQQQ AARAASRWAV QSDSDSDEEV RVVKSAKDKA
LENMERNCVA LKNHMKINDW TQIQTEFDEL VKQLERAKKT LSGLPTFYVR TMVALEDFLL
EKVKNKAEQK KMSKENSKAL IRMKGKIKKQ LEPVRKQIDD FRAHPVGSSE DESSSSESSD
SSDEDSSDES AASSASSKSE KSSDDSESED ESSDDDKSGS DDDSDDSDAS WPSASSSSSS
SSEDDDNMPK GRARWLKQTP VVTKAKKTKG PKVIKQRETR RGSEDEVKKV AVEEELKLTP
SQFDRRVKEV VAMRGKKGMD LSEQLSLMRK LANYARRLGP ARQIVATMYL VGTSVFDTSS
KIDRVMSARH WKQVQTDVCT ILSLLEKNPD FSVAPLTSED QADIVRAGRE KVTAAQIAAA
AAEDAEEDLN FVDTLPQAGK KGTIKVSGDL AAFVDRLTEE YTKSLQQTDP HTSEYVSRLY
DENLLIEVAE RVQNFYARKK DFQRAATMAL VRAELIYYKH DTVAAALFES QAKRAKFGDP
VFLHPACTSS NSNKTKEFDA SKTHPASVMG QPSVDVTPVD AEKLLRDVCR FVFQHGDIRA
KTRAMLCRIY HHALHDRFHE ARDLLLMSHI QDNITDADIP TQILFNRMMA QLGLCAFRCG
LVWEAHACLS EICTGSRTKE LLAQGLQSFR YGERDLEQER LERRRQVPYH MHINLDLLET
CHLVSAMLLE VPNMVNSRLS DRKRMVSKAF RKLLEFHERL VFEGPPENPR DHVVAAAKLL
AQGSWRKSAE LLVGLPVWDL FPGANVSQRV KSMVQHKIQI EALRTYLLAF SAEYDSVSLA
RLMKMFDLDE KTVHSVVSKM MINEELQGAW DQSSQAIVLY KTERSSLQNL AVQYSDKLSQ
IVENNERMMD LRSGTNKEEW GNRGNRGDGR RGAGGRIGFS AGNRRGDNQG GRGGFRPRRG
GGSGGRGPRQ QRQ
//
