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 O84035

Entry ID Method Resolution Chain Position Source
AF-O84035-F1 Predicted AlphaFoldDB

No variants for O84035

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O84035

No associated diseases with O84035

4 regional properties for O84035

Type Name Position InterPro Accession
domain Methionyl/Leucyl tRNA synthetase 6 - 395 IPR015413
domain Methioninyl-tRNA synthetase core domain 5 - 370 IPR033911-1
domain Methioninyl-tRNA synthetase core domain 382 - 393 IPR033911-2
domain Methionyl-tRNA synthetase, anticodon-binding domain 380 - 537 IPR041872

Functions

Description
EC Number 6.1.1.10 Ligases forming aminoacyl-tRNA and related compounds
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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
methionine-tRNA ligase activity Catalysis of the reaction: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).

1 GO annotations of biological process

Name Definition
methionyl-tRNA aminoacylation The process of coupling methionine to methionyl-tRNA, catalyzed by methionyl-tRNA synthetase. The methionyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a methionine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MESSRILITS ALPYANGPLH FGHITGAYLP ADVYARFQRL QGKEVLYICG SDEYGIAITL
70 80 90 100 110 120
NAELAGMGYQ EYVDMYHKLH KDTFKKLGIS VDFFSRTTNT YHPAIVQDFY RNLQERGLVE
130 140 150 160 170 180
NQVTEQLYSE EEGKFLADRY VVGTCPKCGF DRARGDECQQ CGADYEARDL KEPRSKLTGA
190 200 210 220 230 240
ALSLRDTEHA YLHLERMKED LLAFVQGIYL RPHMRNFVTD YIEHLRPRAV TRDLSWGIPV
250 260 270 280 290 300
PDLENKVFYV WFDAPIGYIS GTMDWAASIG DPEAWKKFWL DDTVTYAQFI GKDNTSFHAA
310 320 330 340 350 360
IFPAMEIGQS LPYKKVDALV TSEFLLLEGF QFSKSDGNFI DMDAFLETYS LDKLRYVLAA
370 380 390 400 410 420
IAPETSDSEF SFQEFKTRCN SELVGKYGNF VNRVLAFAVK NGCTELSSPQ LEQKDLDFIS
430 440 450 460 470 480
KSQKLAKDAA EHYAQYSLRK ACSTIMELAA LGNGYFNDEA PWKLAKEGNW NRVRAILFCA
490 500 510 520 530 540
CYCQKLLALI SYPIMPETAL KILEMIAPHS LDLGSQDPDR LQSLWTDSFF DYSEEKFSLK
EPELLFTMVE