Q6FIJ6

PR
Gene name
NIP1
Protein name
Eukaryotic translation initiation factor 3 subunit C
Names
eIF3c, Eukaryotic translation initiation factor 3 93 kDa subunit homolog, eIF3 p93, Translation initiation factor eIF3, p93 subunit homolog
Species
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
KEGG Pathway
cgr:CAGL0M13893g
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-136 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q6FIJ6

Entry ID Method Resolution Chain Position Source
AF-Q6FIJ6-F1 Predicted AlphaFoldDB

No variants for Q6FIJ6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6FIJ6

No associated diseases with Q6FIJ6

3 regional properties for Q6FIJ6

Type Name Position InterPro Accession
domain Proteasome component (PCI) domain 605 - 794 IPR000717
domain Eukaryotic translation initiation factor 3 subunit C, N-terminal domain 88 - 222 IPR008905-1
domain Eukaryotic translation initiation factor 3 subunit C, N-terminal domain 252 - 633 IPR008905-2

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoplasmic stress granule A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress.
eukaryotic 43S preinitiation complex A protein complex composed of the 40S ribosomal subunit plus eIF1A, eIF3, and eIF2-GTP-bound methionyl-initiator methionine tRNA.
eukaryotic 48S preinitiation complex A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA.
eukaryotic translation initiation factor 3 complex, eIF3e An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3e.
eukaryotic translation initiation factor 3 complex, eIF3m An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3m.
multi-eIF complex A multifactor complex composed of multiple translation initiation factors and the initiatior tRNAiMet, which is ready to bind to the small (40S) ribosome to form the 43S preinitiation complex. In S. cerevisiae, this complex is composed of eIF1, eIF2, eIF3, and eIF5.

3 GO annotations of molecular function

Name Definition
RNA binding Binding to an RNA molecule or a portion thereof.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.
translation initiation factor binding Binding to a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.

1 GO annotations of biological process

Name Definition
formation of cytoplasmic translation initiation complex Joining of the large subunit, with release of IF2/eIF2 and IF3/eIF3. This leaves the functional ribosome at the AUG, with the methionyl/formyl-methionyl-tRNA positioned at the P site.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSRFFATNYN YDETSSSSEE DLLSSSEELL SSSEEGELSD DSLFNDESES ESDFDSDDSD
70 80 90 100 110 120
AKPYGPDWFK KPEFRKGGNK FLKGASYSDS DESDEEDGKK VVKSAREKLL DEMQAVYDKI
130 140 150 160 170 180
ETAEMSDDWM TILNEFDSIT RLLVRAQQQN FGIPKIFVKV VAQVEDLVSN SEQTEIKNKA
190 200 210 220 230 240
VSKAFNTTKQ RVKKIARENE ALLAKFREDP QSFDKEDTVE PELPPLNEEN KVFTGKGVNL
250 260 270 280 290 300
SSLASASSEF SFMASLQIVN DSRGKKNSNQ AELIKTLEEL LNIAKTPYER ILAYLTLIPT
310 320 330 340 350 360
RLEESTNLSY QPIDQWKSTH DDLNKLFDIL DENISSYQVT ELAARNDDLE TEPEPNANGI
370 380 390 400 410 420
REILGSLLSF TERLDDEFKK SLLNIDPHSS DYLERLRDEQ NMYNLLLRTQ LYMEATIPEE
430 440 450 460 470 480
RQEQLLARAF VRRLDHIYYK SNKLISIIEN SAWKAVPSSY KSKYIPFSGN ADEEYCSQLV
490 500 510 520 530 540
EGLSKSLANQ DNVFLQKRAT LSHIYYTALN GEFEVAKELL LKTKVQSNIN KSDPSLQILF
550 560 570 580 590 600
NRVVVQLGLS AFKLCKIEEC HQILNELLAS SHLREILGQQ SLQRIASNSS SSSSSEDREK
610 620 630 640 650 660
QCLPYHQHIN LDLVDLVFMT SSLLIEIPQM TAYLTGIKTK KVPVYQKSVR RLVESFDKSF
670 680 690 700 710 720
FHGPPESIKE HVLYAAKSMQ KGDWKGCLEY LKSVKTWNLL PNSVEVLDNL TERIQIETMK
730 740 750 760 770 780
TYVFTYRRFY EKISIKKFSE LFSLPEDKIV TTMEKVIADL ELNIKLDDNK TYIVIEKGDE
790 800
VSKLEEVAVK LNKEIRATRE RLNPSHHNHR