ID A0A1Y2BMH0_9FUNG Unreviewed; 765 AA.
AC A0A1Y2BMH0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=BCR33DRAFT_754884 {ECO:0000313|EMBL:ORY35959.1};
OS Rhizoclosmatium globosum.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Chytridiales;
OC Chytriomycetaceae; Rhizoclosmatium.
OX NCBI_TaxID=329046 {ECO:0000313|EMBL:ORY35959.1, ECO:0000313|Proteomes:UP000193642};
RN [1] {ECO:0000313|EMBL:ORY35959.1, ECO:0000313|Proteomes:UP000193642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL800 {ECO:0000313|EMBL:ORY35959.1,
RC ECO:0000313|Proteomes:UP000193642};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-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}.
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:ORY35959.1}.
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DR EMBL; MCGO01000059; ORY35959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2BMH0; -.
DR STRING; 329046.A0A1Y2BMH0; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000193642; 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; 2.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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:UP000193642}.
FT DOMAIN 623..704
FT /note="PCI"
FT /evidence="ECO:0000259|SMART:SM00088"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 85387 MW; 546446601603E628 CRC64;
MSRFFNKKQA AATQKKIAVA ADSDASSNSE ADSDADSDEN NSMFAAQSSQ SQSQSQKKAA
TSRFGPTAAN SHQRQAFDEM RNIIKPLMNA KKINDWVSIQ NEFDRLNNAY QKVASIQPDE
KLPHPFRFYY RALATLEDAH KAHTESGKTL NAVNQKAFTG MKSKLKKLCK TKEERLRVGE
SGGCCPCCAN GGDGFTSVTK GKPSIDVTPE NLYKKLHELI LARGKKSTDK VVQIEHLSKL
LEVATTAHMK VQVLLVLIPS QFDYNPASTG GFLPADYWKS TRANIDLLLS LLETNHNITI
TETTLLDDVE PAQNEAAFLE GRAVSLRGNL YSFIDRLSDE FIKSLQHIDP HTTEYIERLK
DETPLYVLIV RGQKYFDRLK ATESSDACIL KRVLHIYYKT ENVIAFMESA LPAQSRESTP
AKLVDVLCTA LYQTSDIRIR ARALLCHVYH LALHGKFYEA RDMLLMSHLQ EQVQNTDIDT
QILYNRTVVQ LGMSAFRSGL IRESANALQD FFGSGKTKEL LAQGFQVNNR FGNAASGVAE
KTPEQERLEK QRLLPFHMHI NLELLECIYL TCSMLLEIPN MAMYAHDSRR KMISKPFRRN
LDYNQKQVFI GPPENTRDHI MAAAKSLSAE EGLRTYIFQF APHYDSLGLH QLSAMFDLPV
SAVHSIIAKM IVSEELCASL DEPTQTVVLH RNAPGVEMSR LEYLAGTLVD SNEKMLESRS
IMLGLQQQQQ QQQLNAAGGA KRTVGGGSSG GASGARRTGN KVGFN
//
