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 Q8PYJ4

Entry ID Method Resolution Chain Position Source
AF-Q8PYJ4-F1 Predicted AlphaFoldDB

No variants for Q8PYJ4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8PYJ4

No associated diseases with Q8PYJ4

6 regional properties for Q8PYJ4

Type Name Position InterPro Accession
domain tRNA-binding domain 613 - 715 IPR002547
domain Methionyl-tRNA synthetase, beta subunit, C-terminal 588 - 715 IPR004495
domain Methionyl/Leucyl tRNA synthetase 13 - 400 IPR015413
domain Methioninyl-tRNA synthetase core domain 12 - 375 IPR033911-1
domain Methioninyl-tRNA synthetase core domain 387 - 398 IPR033911-2
domain Methionyl-tRNA synthetase, anticodon-binding domain 384 - 549 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
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 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).
tRNA binding Binding to a transfer RNA.

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
MEIRMSKSSS KPVLVTCGLP YANGKAHIGH LRTYVPADIY ARSLKKEGRE VTFVCGSDTH
70 80 90 100 110 120
GTPIVVNAEE LGITPTELVE IYHKHFDETF KQLGIYFDAF GTTDDPENHN RTHDIVSRLI
130 140 150 160 170 180
EKGYVYPKII EIAYCPACNR FLPDRYVEGA CPHCGETARG DECDQGCGKH LEPGELQNPV
190 200 210 220 230 240
CTICGGPAEY RQQEHFFFKL SEFSNYLMDY LSKDLGGTTN AINYARGWVK QGLTDWCITR
250 260 270 280 290 300
NLEWGVKFPG HEDLVVYVWV DAPIGYIAFT EEWAAQAGDS WEKFWKGDGE IVHFIGGDIT
310 320 330 340 350 360
YHHCIFWPAM LKGADYSVPT AVVASGMVKI EDRKFSKTRG YVVWVGEDYL DHGFHPDLLR
370 380 390 400 410 420
YYLASYTSHT KELNFSWRVL QEKINAELVA VLGNFLYRTM LFAFKNYGEV PEGEVEPEIR
430 440 450 460 470 480
KEIEKALVEV KAAMEEYEFK KAVDSAMALA SFGNTYFQSH EPWKLIKEDR DACGQVVYNC
490 500 510 520 530 540
LHLAKALSLI FEPVIPQTME KAWKGLGHES DIHAALYEET LVPLKAGTKL AKPEILFTKL
550 560 570 580 590 600
EDDRIGEMEE IANQRVAAAN AKRNGVKGGE KEPSKSEGMG PSEASKASEK TVDVATAEEK
610 620 630 640 650 660
VQVETLPVID YEDFAKLDIR VGKVLLVEPV KKSKKLLRIE VDIGEEKPRQ LVAGMASYYT
670 680 690 700 710
PEELVGKSVI VLANLKPAKL CGVESNGMML AADDGGAIVA ALMPDKEIKS GSRIR