Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6CT90

Entry ID Method Resolution Chain Position Source
AF-Q6CT90-F1 Predicted AlphaFoldDB

No variants for Q6CT90

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CT90

No associated diseases with Q6CT90

6 regional properties for Q6CT90

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 170 - 178 IPR000629
domain Helicase, C-terminal 235 - 396 IPR001650
domain DEAD/DEAH box helicase domain 48 - 212 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 42 - 239 IPR014001
domain RNA helicase, DEAD-box type, Q motif 23 - 51 IPR014014
domain ATP-dependent RNA helicase eIF4A, DEAD-box helicase domain 25 - 225 IPR044728

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 A complex of several polypeptides that plays at least two important roles in protein synthesis: First, eIF3 binds to the 40S ribosome and facilitates loading of the Met-tRNA/eIF2.GTP ternary complex to form the 43S preinitiation complex. Subsequently, eIF3 apparently assists eIF4 in recruiting mRNAs to the 43S complex. The eIF3 complex contains five conserved core subunits, and may contain several additional proteins; the non-core subunits are thought to mediate association of the complex with specific sets of mRNAs.
incipient cellular bud site The portion of the budding yeast plasma membrane where a daughter cell will emerge. The yeast marks this spot with bud-site selection proteins before bud emergence occurs. Actin is polarized to this spot just prior to and during bud emergence.
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.

2 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.

2 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.
translation reinitiation A gene-specific translational control mechanism where the small ribosomal subunit remains attached to the mRNA following termination of translation, then resumes scanning on the same mRNA molecule and initiates again at a downstream start site. Reinitiation depends on de novo recruitment of the ternary complex that is required to recognize the next AUG codon.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAPPALRPEN AIRRADELVS VGEPMAALQS LFDLLSSRRS RFADAATLEP IIFKFLELGV
70 80 90 100 110 120
ELRKGKMIKE GLYQYKKHMQ HTPEGLISVG AVARKFIDLI ETKMTNIQAQ TDAKEESNKD
130 140 150 160 170 180
QAEEDLEGGV TPENLLVSVY EQEQTVGGFN NDDVSAWLRF TWESYRTTLD FLRNNSQLEI
190 200 210 220 230 240
TYAGVVNRTM QFCYKYNRKN EFKRLAEMLR QHLDAANYQQ QRYGHHTVDL SDPDTLQRYS
250 260 270 280 290 300
DQRFQQVNVS VKLELWHEAF RSIEDVHHLM RLSKRAPKPS VLANYYENLA KIFFVSGNYL
310 320 330 340 350 360
LHAAAWEKFY NLYLKNPNAS EEDFKFYSSQ FVLSALAIQL DDLPIAGFDP QIRLCDLLDL
370 380 390 400 410 420
ESKPKRKDLI TAAGEQQVVE KADADILKFF NILETNFDVK SAKSQLSALL PNLVEKPYFA
430 440 450 460 470 480
QYVAPLRNLF IRRSIIEVSK AQTSIHLVEL HEMLSLPAPF ELSVFELEKY LIQAAMDDYV
490 500 510 520 530 540
SISIDHETDT VSFAQDPFDA WQASLVEVPE SSTSDEAKNS ESEEETSQET HADEEQNEQV
550 560 570 580 590 600
FTRNSEVRSK LTDLSKILKA NEEYENGSYY YRVKLVREEL IRRKEEVIKL EKEAAEIRAK
610 620 630 640 650 660
SNAERKKRSE EENKILAKKA LEERQRRMAE EKAAVESSME KEAERRAEEM MEREREAIHE
670 680 690 700 710 720
QEMKKLIAET NANGVIHIDP KEAKNLTSDK INQMVIEQVA KNKKDLTERM TYAFKKLDHL
730 740 750 760 770 780
ERAYRQMELP LLEKDAEEQK KRDRENYDNF KKKLIETSKA DYEKKLALHQ RLNKIYSTFN
790 800 810 820 830 840
QYKSSVIAEK KEELEKQRAL KEAQLEEAKK QRIEQVRKER YEAKVAEIQA AIEAEAAEKE
850 860 870 880 890 900
ALAKEEELAK RRAERERINK ERDEIARKQR EIEELLEKKN GSSRSSPVPS TPTPAPAPAQ
910 920
TAPVSNKPMS MAEKLRLKRM NAGRG