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 Q26228

Entry ID Method Resolution Chain Position Source
AF-Q26228-F1 Predicted AlphaFoldDB

No variants for Q26228

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q26228

No associated diseases with Q26228

5 regional properties for Q26228

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 159 - 497 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 64 - 142 IPR004365
domain Aminoacyl-tRNA synthetase, class II 180 - 495 IPR006195
domain Lysyl-tRNA synthetase, class II, C-terminal 173 - 498 IPR018149
domain Lysine-tRNA ligase, class II, N-terminal 63 - 170 IPR044136

Functions

Description
EC Number 3.6.4.12 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus
  • Chromosome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
chromosome A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information.
Ku70:Ku80 complex Heterodimeric protein complex composed of a 70 kDa and a 80 kDa subunit, binds DNA through a channel formed by the heterodimer. Functions in DNA double stranded break repair, chromosome maintenance, transcription regulation, V(D)J recombination, and activation of DNA-PK.

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.
damaged DNA binding Binding to damaged DNA.
DNA helicase activity Unwinding of a DNA helix, driven by ATP hydrolysis.
telomeric DNA binding Binding to a telomere, a specific structure at the end of a linear chromosome required for the integrity and maintenance of the end.

3 GO annotations of biological process

Name Definition
DNA recombination Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
double-strand break repair via nonhomologous end joining The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
telomere maintenance Any process that contributes to the maintenance of proper telomeric length and structure by affecting and monitoring the activity of telomeric proteins, the length of telomeric DNA and the replication and repair of the DNA. These processes includes those that shorten, lengthen, replicate and repair the telomeric DNA sequences.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDQPWMRQDD DESDDESSTV DFGQAVDGIL FLIDATEGMF EEVDGDTAFM QCIKAAKSTM
70 80 90 100 110 120
LNKITSSPKD LVGIILFGTD KDNNPNRFKN VYVLQDLESP GAESVLKLEK LIADGPKKFK
130 140 150 160 170 180
QEYGHGNVNM ADVLWTCALM FSKSRAGQRR VLVLTNQDDP HKGSGDLDDK AVVKAKDLLQ
190 200 210 220 230 240
SGIELDLVHL KPPGDKKFRP QILYKNLVTD KENYEDGFPE ASDKMEELLL RVRMKDHKKR
250 260 270 280 290 300
RLMSLPFWLG PEVKMSVSLY NLVRPTGKPA TTRLARDNNE ELLSRRITYA MDSAEALMPG
310 320 330 340 350 360
DISKTQEYGG RKAYFDICEV KQIKSMAPPG LQLLGFKPLS YLEKQPHVRP SHFVYPDEGS
370 380 390 400 410 420
VRGSTRLFAA LLQSCLRHRV APICFWISRA AQAPKLVYLL AQEEERDPHG LQMVPPGFHV
430 440 450 460 470 480
VQLPFSDDRR RLQALQEGTT KATPGLVALA REMAEKLRFT YHPDKFENPE LQGFWSCLEA
490 500 510 520 530 540
LALDRDDAEH PKDYTRPDHE KMKAKAGEEM DAFLEAAFPD GCSATTAGSR KRTQAGEGGQ
550 560 570 580 590
AKKARSENQG SNVDVREEAK RGKLASLTVS VLRDFCKQEG LRCPSKKAEI VDCIKKHLKL