ID A0A094GRR6_9PEZI Unreviewed; 1341 AA.
AC A0A094GRR6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=V501_08045 {ECO:0000313|EMBL:KFZ05770.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ05770.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ05770.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFZ05770.1}.
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DR EMBL; JPKD01002264; KFZ05770.1; -; Genomic_DNA.
DR STRING; 1420914.A0A094GRR6; -.
DR HOGENOM; CLU_004304_1_0_1; -.
DR Proteomes; UP000029315; 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:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
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 GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR046825; PDH_C.
DR InterPro; IPR003099; Prephen_DH.
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; PF03446; NAD_binding_2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF20463; PDH_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
DR PROSITE; PS51176; PDH_ADH; 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}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000029315}.
FT DOMAIN 4..285
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 1063..1237
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 467..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 629..656
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 475..511
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1341 AA; 150668 MW; A292AFDAFDD2694F CRC64;
MENFVVGIIG MGDMGKMYAR QLSDAGWRVN ACDREEKYLD LVDEFSSRKQ VEILRNGHLV
SRASDYIIYN VEAASIDKVV ALYGPSTKQG AVVGGQTSCK SPEIAAFEAH LPKDVDIVSC
HSLHGPNVDP KGQPLVLIKH RASQANFDRV EKVLSCLGSQ HVYLSATEHD RITADTQAVT
HAAFLSMGKA WHANAQFPWE IARYVGGIEN VKINLTLRIY SQKWHVYAGL AILNPYAKEQ
IRQYSQSVTD LFKLMLGGNR EEFERRIRAA GAAVFDAQKS HHGILLEDEV LDRFSLGKKP
DEPTPNNHLS LLAMVDCWSR MGIVPYDHMI CSTPLFRLWL GVTEYLFRKP ALLDDVIRIA
IEDNTFRSDD LEFTFAARGW SDCVTFGDFE SYKDRFESTR KFFEPRFADA TKGMERSLAS
IKISAGTQPQ FLTLKTATTS VRALHLRTYN VKGSALVLNK MSSKFFRTGD DTSSESSSEE
EEELYSESEE EEQEASESGS EKEDEEESES EDEKAGGKKT GAMAFFRGAG SDDDESTDDE
QVHVVKSAKD KRLEELEATS KAIENGKKIN DWGSISAEFD KINRQVVKLL QSGSMPKLYI
KAIAELEDFM NETIAKQKVT AKKMNATNAR GLNAVKQRIK KNNKDYQKDV DAYRADKDAF
MESEEEEEVV VVKKPGKAAV SFALDEEPGA DDGFHTVGKG GRTLQFTPES ILKHLRSIME
SRGKKNTDRT EQIKIMEKLY EVATTPYQKI RVLLTLISTR FDLSTGAQTF MSQEQWKAAE
QEFGTLLTIL ESNLDLVVVE NAEEWEDDEK QPVPVAGEKL KIPGSVVSYI ERLDDELTRS
LQHIDPHTAE YIDRLSDEGS LYNSIVRTQL YVEVMTKDTT LEIPQDNTNR IIMRRLEHVY
FKPATVVKIL EENCWKSIPA SLQSTITPQT QTPDATALVN VLCNYLFIHS EGIIRARAML
CQIYFLALHD NYYKARDMML MSHLQETISN FDVNSQILFN RTLVQVGLCA FRAGLVYEAQ
NTLQEICGSG RQKELLAQGV MIQRYNQVSP EQERLERQRQ LPFHMHINLE LLECVYLTCS
MLLEIPLLAQ TGSSPDIKKR VISKTYRRML EYHERQIFTG PPENTRDHVM QASKALAAGE
WQKATEFIHS IKIWELMSKP DAIKTMLSEQ IQEEGLRTYL FTYAPFYDTL SVATLSSMFE
LSNRKVAAIV SKMISHEELA AALDQVNSSI IFRKGVELSR LQSLALTLSD KASGLIESNE
RTLETRTQGT ANAFERQGGR GGRGGGRGGQ RGGRGGGRGG GPNTQRQEGG TRFTGGALGA
AVRAHRDLHL NVRDSSLTDH I
//
