ID A0A1X2HND4_SYNRA Unreviewed; 794 AA.
AC A0A1X2HND4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BCR43DRAFT_453039 {ECO:0000313|EMBL:ORZ00858.1};
OS Syncephalastrum racemosum (Filamentous fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX NCBI_TaxID=13706 {ECO:0000313|EMBL:ORZ00858.1, ECO:0000313|Proteomes:UP000242180};
RN [1] {ECO:0000313|EMBL:ORZ00858.1, ECO:0000313|Proteomes:UP000242180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORZ00858.1,
RC ECO:0000313|Proteomes:UP000242180};
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:ORZ00858.1}.
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DR EMBL; MCGN01000002; ORZ00858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2HND4; -.
DR STRING; 13706.A0A1X2HND4; -.
DR InParanoid; A0A1X2HND4; -.
DR OMA; FRCGLIK; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000242180; 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:UP000242180}.
FT DOMAIN 591..762
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 90076 MW; E716C12DD8D3A0D5 CRC64;
MSRFFRSGSD SESETDSSDN ESFISDEELS SEEEDELSAD EQQQDDQPSK KSRFLKDADS
ESEDESDEEI GGKRRAKSAK DKREELMQSS AKAIENGQKN NDWVLISSEF DKLIISVQKA
TTGFDKIPVP KFFVKILVEL EGLVNEAQKE KTGGKKKPSP NAKAQLGMKQ KLKKSTKPYE
ALMAEYKKDP EAFMAEPEVT PVAPSPQRVS SPAVGQTVTE AELDGFSAVG KKGRTVTAVA
APPKEENLFV RLREVLENRG KKNTNRDEQI ATLEELLGAA ESPFQKILVL LALIPSRFDF
NQSMTEHMQV DIWKKVEVEI SSLLEILETN PSYVIRETAE ELDHEDKDVV PEEGKTVGIP
GSVVSLVERL DDEFTKSLQS IDPHTTEYID RMRDEPGLYA VLVRVQAYVE RHHMSESLPR
IVLRRLEHLY YKPEQVIQST EKIAKSRLPE YITSSVTTAE EPSQLIHEMC TYLYKQDVSV
IRTRAMLCHI YHIALHRQFH TARDMLLMSH LQESVHQADI LTQVLYNRTV VQIGLCAFRD
GLIKEAHACL QEIQGSGRVK ELLAQGVQAS RFGQQMTPEL EQLERQRQLP FHMHINLELL
ECVFLTCSML LEIPAQAQAG PNNKKMISRP FRRLLDYNER QAFTGPPENT RDHIMSAAKA
LASGEWERAR DYILAIKIWN LMPENQQIKD MLVAKIQEEG LRTYLFTYAS YYSTIGLAQL
ASMFALSESR VSAIVAKLIW NEELSASLDQ VAQCVVLHRV EPSRLQVLSM QFSEKAANLV
DQNERLLTTG RDRQ
//
