ID A0A2X0LUV3_9BASI Unreviewed; 945 AA.
AC A0A2X0LUV3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BQ5605_C010g06179 {ECO:0000313|EMBL:SGY14425.1};
GN Synonyms=NIP1 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=BQ5605_C010G06179 {ECO:0000313|EMBL:SGY14425.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY14425.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY14425.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQNC01000012; SGY14425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0LUV3; -.
DR STRING; 796604.A0A2X0LUV3; -.
DR Proteomes; UP000249464; 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:UP000249464}.
FT DOMAIN 684..858
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..139
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 104964 MW; 5C91F576F5A4DFCA CRC64;
MHSSPLESPR DRRHAPLRSV SGKRGEKGSG VDHRTTITFH SNRHFFFPQK SDFDPFTDPI
PLVPCPVSSF FRSVSDSSDS SSDEEEELLS DDSGDDSGLE GKTALSKPKG SRFLKSTGDD
SDDSGSDDDD DDDSDQDGSD DDKAAAKKPI GSRFLKGAAS DDSDSDDERT KVVKSAKSKR
ADEVESCVKA IENAARINDW SAISDQFDKL VRLVSRQANV AEPVPSGFIK ALVSLDDHLA
SAQGAKKKMN ATNAKALNSM KQKLKKTQRE HDETIKKYKQ DPDAFEKAAA LEDQPAAAAA
PKKAKKATQA VDEEADDDFQ TVGSKGKTIN VTSEGIYKAL SQVMEARGRK NTDRTEQSKI
LDRLLAVAVS PYQKIRVLLA LISALLDYNP STNTHMPLDA WSAARTHLDS LLDILVQQRD
HVVAEDAPDY DDQVERAPSA SEPTIIVRGS VISLVDRLDD EFTRSLQHID PHTSEYIERL
KDERAIYETI VKAQVYYEQT RLIEHLDRVV TRRLEHVYCK PDVVAQALES TLPALSSQSK
IWSTAASSSG ASSFSAVALV RALCIHLYKT ENSLLRTRAM LCHIYHHALH DQYHTARDML
LMSHLQDTVG SADVGTQILY NRTVVQVGLC AFRLGLIRES QSTLQEIFAT QRVKELLAQG
VQAQRYSVLT PEQDKLERQR QLPFHMHINL ELLECAYLVA SMLLEVPLMA QAGNDPEMRK
RVVSRTFRRM LDYANRQAFT GPPENKRDHV MQATKALQQG DWQRCVDLIH SIKVWNLMPS
ERKVKEMLKR KIQEEGLRTY VFTYAPFYST LSLEQLASTF ELPLATATSL VSKMIWNEEL
DASLDQVSRV VVLQSTEVTA LQRLALQLAD KASQMADNSE RYLDSKLQSG ESRADGVRAE
RTEGNDTRPR RGGGGGGRGR GSRGGGRGGA SRQFQTGTLG RTVQA
//
