A1D558

PR
Gene name
prt1 (NFIA_022620)
Protein name
Eukaryotic translation initiation factor 3 subunit B
Names
eIF3b, Eukaryotic translation initiation factor 3 90 kDa subunit homolog, eIF3 p90, Translation initiation factor eIF3 p90 subunit homolog
Species
Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
KEGG Pathway
nfi:NFIA_022620
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

594-700 (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 A1D558

Entry ID Method Resolution Chain Position Source
AF-A1D558-F1 Predicted AlphaFoldDB

No variants for A1D558

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1D558

No associated diseases with A1D558

3 regional properties for A1D558

Type Name Position InterPro Accession
domain RNA recognition motif domain 40 - 126 IPR000504
domain Translation initiation factor, beta propellor-like domain 401 - 623 IPR013979
domain eIF3B, RNA recognition motif 39 - 122 IPR034363

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.

4 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
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
MAPSFDTLSE QDLHEEEEEE IDFSDLKAQY EVKLEEGLDT FVVIDGLPVV PEESRQKLIK
70 80 90 100 110 120
FLLRKLNTVG HTSEDAVFMP LNDKNMSEGY AFVEFETPEQ AVAAVKQLHG TPLDKKHTLL
130 140 150 160 170 180
VNKLMDIERY GREGRIDEEY KPPAIEPFKE KEHLRSWLAD PNARDQFALH RGDKVGVFWN
190 200 210 220 230 240
NKNNPPENVV DRAHWTQLFA QWSPKGTYLA SVHPQGVQLW GGPAFSKQKQ FPHPFVQLIE
250 260 270 280 290 300
FSPGESYLTT WSARPIQVEE GQSILTYEEE GKNIIVWDIA TGKPLRSFVS HDLTAGPAGD
310 320 330 340 350 360
AEPKKKVQWP AFKWSADEKY VARMLQHQSI SIYELPRMNL LGKTSVKIDG VMDFEWSPAT
370 380 390 400 410 420
VTREGVKQYE QLLCFWTPEI GSSPARVAMM SVPSKEIVRT RNLFNVSDVK LHWQSQGSYV
430 440 450 460 470 480
CVKVDRHSKS KKSMATNLEI FRVREKGVPV EVVDSLKDTV INFAWEPNGN RFVLITTGEA
490 500 510 520 530 540
VAGAAVAPKT AVSFFAPEKK GGAIGNFKLI RTIEKKNSNA IYWSPKGRFV VVATVHSQTS
550 560 570 580 590 600
FDMDFWDMDF EGEKPEAEKD FAANLQLMKT IEHYGVTDID WDPTGRYVVS SASVWTHQLE
610 620 630 640 650 660
NGWNMHTFAG QTLSENPTDK FKQFLWRPRP PTLLSKEEQK QVRKNLREYS KEFDEEDRYA
670 680 690 700 710 720
VDIANTAVVE KRKRVLNEWV AWIRREKELL AEEKDAYGLP EEADDPKLAK DAAATTQEQG
730
ETVVEEIVEE IIEESEEVIG