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 Q6CX73

Entry ID Method Resolution Chain Position Source
AF-Q6CX73-F1 Predicted AlphaFoldDB

No variants for Q6CX73

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CX73

No associated diseases with Q6CX73

5 regional properties for Q6CX73

Type Name Position InterPro Accession
conserved_site ATP-dependent RNA helicase DEAD-box, conserved site 170 - 178 IPR000629
domain Helicase, C-terminal 237 - 398 IPR001650
domain DEAD/DEAH box helicase domain 48 - 213 IPR011545
domain Helicase superfamily 1/2, ATP-binding domain 42 - 241 IPR014001
domain RNA helicase, DEAD-box type, Q motif 23 - 51 IPR014014

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus, nucleolus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
FAL1-SGD1 complex A protein complex involved in the 18S rRNA biogenesis. In S. cerevisiae this complex consists of Fal1p and Sgd1p and in humans this complex consists of NOM1 and eIF4AIII subunits.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
preribosome, small subunit precursor A preribosomal complex consisting of 20S pre-rRNA, ribosomal proteins including late-associating small subunit proteins, and associated proteins; a precursor of the eukaryotic cytoplasmic small ribosomal subunit.
small-subunit processome A large ribonucleoprotein complex that is an early preribosomal complex. In S. cerevisiae, it has a size of 80S and consists of the 35S pre-rRNA, early-associating ribosomal proteins most of which are part of the small ribosomal subunit, the U3 snoRNA and associated proteins.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
RNA binding Binding to an RNA molecule or a portion thereof.
RNA helicase activity Unwinding of an RNA helix, driven by ATP hydrolysis.

2 GO annotations of biological process

Name Definition
maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Any process involved in the maturation of a precursor Small SubUnit (SSU) ribosomal RNA (rRNA) molecule into a mature SSU-rRNA molecule from the pre-rRNA molecule originally produced as a tricistronic rRNA transcript that contains the Small Subunit (SSU) rRNA, 5.8S rRNA, and the Large Subunit (LSU) in that order from 5' to 3' along the primary transcript.
RNA biosynthetic process The chemical reactions and pathways resulting in the formation of RNA, ribonucleic acid, one of the two main type of nucleic acid, consisting of a long, unbranched macromolecule formed from ribonucleotides joined in 3',5'-phosphodiester linkage. Includes polymerization of ribonucleotide monomers. Refers not only to transcription but also to e.g. viral RNA replication.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSFNRDDDSK LKFKTSKKLK VSATFESMNL KPDLLRGIYF YGFEYPSSIQ SRAISQIISG
70 80 90 100 110 120
KDVIAQAQSG TGKTATFTIG LLQAIDSKSK ELQALVLSPT RELASQSESV ISNLGDYLNV
130 140 150 160 170 180
TAHACTGGKA LQQDIKKVSK NCQVVSGTPG RVLDMIKRQV LNVRNCKILV LDEADELLGE
190 200 210 220 230 240
TLGFKQQIYD IFTKLPPTIQ VVVVSATMSK DILEITKKFM SDPVKILVKR DEISLDVIKQ
250 260 270 280 290 300
YYVDVEKEEW KFDTLCDLYD SLTITQCVIF CNTRKKVDWL SRKLTQTNFS VSSMHGDMKQ
310 320 330 340 350 360
EERDQVMNDF RSGKARVLIS TDVWARGIDV QQISLVINYD IPDNLENYIH RIGRSGRFGR
370 380 390
KGVAINFITK EERPKLKEIE SHYRIKIKPT PANLEELS