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 Q3Z9C5

Entry ID Method Resolution Chain Position Source
AF-Q3Z9C5-F1 Predicted AlphaFoldDB

No variants for Q3Z9C5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3Z9C5

No associated diseases with Q3Z9C5

5 regional properties for Q3Z9C5

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 51 - 62 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 22 - 567 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 610 - 752 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 820 - 878 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 572 - 698 IPR033705

Functions

Description
EC Number 6.1.1.9 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.

3 GO annotations of molecular function

Name Definition
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
valine-tRNA ligase activity Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
valyl-tRNA aminoacylation The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-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
MAQCSGLPEM AKAYEAAEVE KKWYQYWMEK GYFKPNPDSD KKPFVIIMPP PNVTGELHLG
70 80 90 100 110 120
HALTATLEDI MIRWHRMLGE PALWLPGADH AGIAAQVVVE RMLAKQGKTR QELGRELFLE
130 140 150 160 170 180
KMWEWVNPCR ERIRHQHMRL GASCDWDRET FTLDPGPVKA VREIFTNLYQ KGLIYRGERI
190 200 210 220 230 240
INWCPRCATA VSDLEVDHKD LAGHIWHLRY PLEDGSGFVT VATTRPETML GDTAVAVHPD
250 260 270 280 290 300
DARYTGMVGK NVLLPIMNRR IPVIADEAVD MAFGTGAVKV TPAHDPNDFE MGLRHSLPMI
310 320 330 340 350 360
TIQNRDTTMN ENAGPCSGMT AKACREYVVS ELKSLGLLLK IEDYTHSVGH CQRCSAVIEP
370 380 390 400 410 420
MVSKQWFVKM EPLAKPALEA VNSGRIQILP ERFTKVYQNW MENIRDWCIS RQLWWGHRIP
430 440 450 460 470 480
VWYCPCGEMI VSKEDPTACP KCGSTKLEQD PDVLDTWFSS GLWPHSTLGW PDQTEDLKRF
490 500 510 520 530 540
YPGSVLETAY DIIFFWVARM IVMGIEDMKE VPFRTVYLHG LIRDDKGEKM SKTKGNVIDP
550 560 570 580 590 600
LKVIDQYGTD ALRFAVTFGT SPGNDSKLGQ TKLEAARNFV NKLWNASRFV IMNLGEEKEL
610 620 630 640 650 660
LPEAGLPLED RWILSRMNRV TADVIRLMEE FQFGEAQRVL QDFVWGEFCD WYIELAKVRL
670 680 690 700 710 720
RDEASVSPRP VLVKVLSTIL RLLHPYMPFI TEELWSYLRP YLPKSLGETD IIVAPFPQAD
730 740 750 760 770 780
ETCFDEQAES IMGSLVEVVR SLRNLRAEHN VEISRYIQAN IYAGDMAEVL SNYLGAVETL
790 800 810 820 830 840
SRSRPVNILP GHYSGASTAT EVVLVLNGIE VVVPMSTMVD LEAEAKRVEA EIAELETQIE
850 860 870
RLSARLSDTQ FLAKAPQAVV DKERTKLEGY IEKVSRLKAV