Q58530

PR
Gene name
MJ1130
Protein name
Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
Names
Species
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
KEGG Pathway
mja:MJ_1130
EC number
2.3.1.234: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

279-358 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

5 structures for Q58530

Entry ID Method Resolution Chain Position Source
2VWB X-ray 305 A A/B 1-535 PDB
3EN9 X-ray 267 A A/B 1-535 PDB
3ENH X-ray 360 A A/B 1-535 PDB
5JMV X-ray 339 A A/B/C 1-335 PDB
AF-Q58530-F1 Predicted AlphaFoldDB

No variants for Q58530

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q58530

No associated diseases with Q58530

4 regional properties for Q58530

Type Name Position InterPro Accession
domain Protein kinase domain 333 - 535 IPR000719
domain Gcp-like domain 1 - 323 IPR000905
active_site Tyrosine-protein kinase, active site 447 - 459 IPR008266
conserved_site Peptidase M22, conserved site 91 - 111 IPR017860

Functions

Description
EC Number 2.3.1.234 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
EKC/KEOPS complex A protein complex involved in t6A tRNA modification. For example, in Saccharomyces cerevisiae the complex contains Bud32p, Kae1p, Gon7p, Cgi121p, and Pcc1p.

8 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
iron ion binding Binding to an iron (Fe) ion.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
N(6)-L-threonylcarbamoyladenine synthase activity Catalysis of the reaction: L-threonylcarbamoyladenylate + adenine(37) in tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.
protein serine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate.
protein serine/threonine kinase activity Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
protein serine/threonine/tyrosine kinase activity Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
protein phosphorylation The process of introducing a phosphate group on to a protein.
tRNA threonylcarbamoyladenosine modification The attachment of a carbonyl group and a threonine to the amino group of the adenine residue immediately 3' of the anticodon, in tRNAs that decode ANN codons (where N is any base).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MICLGLEGTA EKTGVGIVTS DGEVLFNKTI MYKPPKQGIN PREAADHHAE TFPKLIKEAF
70 80 90 100 110 120
EVVDKNEIDL IAFSQGPGLG PSLRVTATVA RTLSLTLKKP IIGVNHCIAH IEIGKLTTEA
130 140 150 160 170 180
EDPLTLYVSG GNTQVIAYVS KKYRVFGETL DIAVGNCLDQ FARYVNLPHP GGPYIEELAR
190 200 210 220 230 240
KGKKLVDLPY TVKGMDIAFS GLLTAAMRAY DAGERLEDIC YSLQEYAFSM LTEITERALA
250 260 270 280 290 300
HTNKGEVMLV GGVAANNRLR EMLKAMCEGQ NVDFYVPPKE FCGDNGAMIA WLGLLMHKNG
310 320 330 340 350 360
RWMSLDETKI IPNYRTDMVE VNWIKEIKGK KRKIPEHLIG KGAEADIKRD SYLDFDVIIK
370 380 390 400 410 420
ERVKKGYRDE RLDENIRKSR TAREARYLAL VKDFGIPAPY IFDVDLDNKR IMMSYINGKL
430 440 450 460 470 480
AKDVIEDNLD IAYKIGEIVG KLHKNDVIHN DLTTSNFIFD KDLYIIDFGL GKISNLDEDK
490 500 510 520 530
AVDLIVFKKA VLSTHHEKFD EIWERFLEGY KSVYDRWEII LELMKDVERR ARYVE