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 A5DB98

Entry ID Method Resolution Chain Position Source
AF-A5DB98-F1 Predicted AlphaFoldDB

No variants for A5DB98

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5DB98

No associated diseases with A5DB98

2 regional properties for A5DB98

Type Name Position InterPro Accession
domain PAP/25A-associated 322 - 381 IPR002058
domain Polymerase, nucleotidyl transferase domain 160 - 268 IPR002934

Functions

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

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

5 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.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSQEFNEIDA NTIETNYDNV VYSFDDLNLK PNIVRGIFGY GYESPSAIQQ RAILPITEGR
70 80 90 100 110 120
DVLAQAQSGT GKTATFTISA LQRIDENLKA TQALILAPTR ELALQIQNVI THIGLYLNVT
130 140 150 160 170 180
VHASIGGTSM KDDIEAFKSG VQIVVGTPGR VFDMIERRFF RTDKVKMFIM DEADEMLSSG
190 200 210 220 230 240
FKEQIYNIFR LLPETTQVVL LSATMPQDVL EVTTKFMNNP VRILVKKDEL TLEGIKQFYI
250 260 270 280 290 300
NVEQEDFKFD CLCDLYDSIS VTQAVIFCNT RSKVEFLTTK LKAENFTVSA IHADLPQSDR
310 320 330 340 350 360
DTIMNEFRSG SSRILIATDL LARGIDVQQV SLVINYDLPA NKENYIHRIG RGGRFGRKGV
370 380 390
AINFVTDEDV GMMREIEKFY STQIEEMPAN IGELFN