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Database: UniProt
Entry: K5WVC4_PHACS
LinkDB: K5WVC4_PHACS
Original site: K5WVC4_PHACS 
ID   K5WVC4_PHACS            Unreviewed;       870 AA.
AC   K5WVC4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=PHACADRAFT_258172 {ECO:0000313|EMBL:EKM54372.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM54372.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM54372.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM54372.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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; JH930473; EKM54372.1; -; Genomic_DNA.
DR   RefSeq; XP_007397066.1; XM_007397004.1.
DR   AlphaFoldDB; K5WVC4; -.
DR   STRING; 650164.K5WVC4; -.
DR   GeneID; 18917043; -.
DR   KEGG; pco:PHACADRAFT_258172; -.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; K5WVC4; -.
DR   OrthoDB; 5482362at2759; -.
DR   Proteomes; UP000008370; 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   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:UP000008370}.
FT   DOMAIN          607..780
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          158..211
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        69..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..845
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   870 AA;  98637 MW;  DEE591CE2B974BA1 CRC64;
     MSRFFRQAGD SDSETESSSE EELMSSEDEA PKPATTKPAM SRFLRGAGNS DSSDGSDSES
     ESESESSEEE DDKTKKKSRF LRTEEDEDSS DEEEGKRVVK SARDKRLEEM EASGKMMDNA
     LKINDWVAIS NEFDKLHRMV QRQQNVSEPV PPFFIRTLVN LESSLNAAVS KEKEAKKKMN
     ASNARALTAM KQKVKKVLKE FEIETKKFQE DPEAFEREYS AAVTVEAPSV QKAKRGKKAE
     EGTEDEEDFT TVGKGGKTIQ FTPESIFKNL QAIQEARGKK NTDRSEQIRI LEKLLEISVT
     SYQRIRVLLA LISSRFDYNS SVATHMPIDL WIAAQKEVDQ LVGVISQDPR YSIQEVTNDY
     DELAERSPET EPNGTVVIRG SVISFMDRLD DEFTKSLQNI DPHGTEYVDR LKDEKNLYCT
     ICRAQALYEK TKQDEPLGRI VMRRLEHIYS KPDAVVQALE STVAVSDLKP SILLSEFATK
     DLIHRLCVHL YKSGNSLLRT RAMLCHIYHY ALHNDFHTAR DMFLMSHLQE SIHTADVATQ
     ILYNRTVVQL GLSAFRCGLI KESQAILQDI FATQRVKELL AQGVHTQRYQ VLTPEQEKAE
     RQRQLPFHMH INTELLEAAF LVSSMLVEIP LLASIDNEEQ KRKTISKSFR RLLDFADRQV
     FTGPPESTRD HIMQASRALQ DGEWEKCRDF VQSIKIWSLM PEAASVKEML AKRIQEEGLR
     TYLFTYAPHY STLSLSLLSR TFSLPLRAVT SIVSKMIWSE ELSASLDQQA GAVVFHRIEL
     SRSQLLAQVL ADKVNAMVEQ NEKTLDQKLG NVTSWSDRQD GAKGDKREQA GERRRGAERR
     GGVRGGTRGG RGARFAQGLG NQMASAQRSR
//
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