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 Q0W0H2

Entry ID Method Resolution Chain Position Source
AF-Q0W0H2-F1 Predicted AlphaFoldDB

No variants for Q0W0H2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0W0H2

No associated diseases with Q0W0H2

6 regional properties for Q0W0H2

Type Name Position InterPro Accession
domain tRNA-binding domain 583 - 683 IPR002547
domain Methionyl-tRNA synthetase, beta subunit, C-terminal 543 - 683 IPR004495
domain Methionyl/Leucyl tRNA synthetase 16 - 401 IPR015413
domain Methioninyl-tRNA synthetase core domain 15 - 376 IPR033911-1
domain Methioninyl-tRNA synthetase core domain 388 - 399 IPR033911-2
domain Methionyl-tRNA synthetase, anticodon-binding domain 385 - 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
MIEEKLMSEF PCDKPVLVTC GLPYANGSAH IGHLRTYIPA DMFVRTLRMM GQETVFVCGS
70 80 90 100 110 120
DAHGTPIIVN AEEQKISPRQ LVDKYHVQFD SIFKKCGVIF DRYGNTDDPT NHARTKSIVS
130 140 150 160 170 180
ELQKNGYVYP KEIKVAYCPQ CQRGLPDRYV EGVCPYCSSI ARGDECDIGC QRHLEPGEIL
190 200 210 220 230 240
DPKCKVCGSK AEVRTQEHFF FKLSEFGDFL QEYLNTLHAT PNAVNYAMEW AKELKDWCIT
250 260 270 280 290 300
RNLEWGVKYP GHEDLVVYVW VDAPIGYIAF TEEYAKAAGK NWEDLWKGDS RIIHFIGGDI
310 320 330 340 350 360
IYHHCIFWPA MLKGAGYTLP WGVVASGMIK VNDKKFSKSR GYIVWVEDDY LAHGFHPDLL
370 380 390 400 410 420
RYYILSYTSH TKDINFSWTE FQTKINKELV GSYGNFVNRV LTFIDSKGID VKGTIDPKIS
430 440 450 460 470 480
SAIKTAIDMV KTEIGNYEFK KICDSIITLS DVGNTYFQSH EPWKLIKENP AACENVLFNC
490 500 510 520 530 540
IQIVKALAIL SEPTVPEKAK EIWGMLGYDP ATLASARIDD ALVPYENRPR PKPSILFTKL
550 560 570 580 590 600
EDKKIAEMTK IMDERVKAAE AKLNGKKAEE ELEPQLPPIT IDDFAKMELR VGKVIASEKI
610 620 630 640 650 660
KGSKKLLKNL IDLGEDKPRQ IVSGIAEVYT PEEMVGKTVI VIANLKPTKI MGVESNGMIL
670 680
AADSNGATLL TVEKPSEPGT KVR