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 A2SRE2

Entry ID Method Resolution Chain Position Source
AF-A2SRE2-F1 Predicted AlphaFoldDB

No variants for A2SRE2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2SRE2

No associated diseases with A2SRE2

6 regional properties for A2SRE2

Type Name Position InterPro Accession
domain tRNA-binding domain 575 - 673 IPR002547
domain Methionyl-tRNA synthetase, beta subunit, C-terminal 543 - 673 IPR004495
domain Methionyl/Leucyl tRNA synthetase 7 - 391 IPR015413
domain Methioninyl-tRNA synthetase core domain 5 - 366 IPR033911-1
domain Methioninyl-tRNA synthetase core domain 378 - 389 IPR033911-2
domain Methionyl-tRNA synthetase, anticodon-binding domain 375 - 540 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
MTNKPTVVTC GLPYTNGFCH LGHLRTYIPG DFYVRYLRRL GDDIVFICGS DNHGTPIVVT
70 80 90 100 110 120
AEAEKTTPRA VSETYHAHFD NVFKSMGIAF DRFGMTDDPT NHHRTVSILQ TLIDRGYVYE
130 140 150 160 170 180
QTIQQSYCPK CKRFLPDRYV EGTCPYCGKH ARGDECDSGC GRHLEPGEIL DPVCATCGTK
190 200 210 220 230 240
AELREQKHYY FKLSSFRDYL LEYLPTLGGT LNAKNYAIGW VENELKDWCI TRMMDWGVKF
250 260 270 280 290 300
PGSDDLVCYV WVDAPIGYIS FTEEWAKATN NSWQKYWCEG DRVHFIGSDI IYHHCVFWPA
310 320 330 340 350 360
MLHGAGYQPP TAVVASGMVT IDGEKFSKSK GNVVWTKEDY LDKGLPADYL RYYLLAYTSH
370 380 390 400 410 420
TRELDFSWKE FQARINNELV NTFGNFANRS MSLVKTKFGD VPQVPVEAEI FAEIERSLAA
430 440 450 460 470 480
IEESVRAYEF KAAVDGILLL AAYGNSYISN AAPWKLIKED PQAAAQILKN CLQIVKACAL
490 500 510 520 530 540
IMQPVMPESS QKLWEMLGYT DKIESRPISD ALVPFENTTL GDVKPLFARI EDKQREEMEA
550 560 570 580 590 600
VLTKRAEDSK KKAAGKNTME AVIEPISEEI ITIDDVAKLD LRVGRVVKAE RVPKTTKLLR
610 620 630 640 650 660
LQVDIGTEVR QIVSGIADVY TPEEMVDKKI IVVVNLKPAK FRGEESNGML FAAGEEASLL
670
VPLKDVPEGT KVH