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 Q3ZZG9

Entry ID Method Resolution Chain Position Source
AF-Q3ZZG9-F1 Predicted AlphaFoldDB

No variants for Q3ZZG9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3ZZG9

No associated diseases with Q3ZZG9

5 regional properties for Q3ZZG9

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 - 879 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
MAQCSDLPEM AKAYEAAEVE KKWYQYWMEK SYFKPNPNSD KKPFVIIMPP PNVTGELHLG
70 80 90 100 110 120
HALTATLEDI MIRWHRMQGE PTLWLPGVDH AGIAAQVVVE RELAKQGKTR QQLGRELFLE
130 140 150 160 170 180
KMWEWVNPCR EKIRHQHMRL GASCDWDRET FTLDAGPVKA VREIFTNLYE KGLIYKGERI
190 200 210 220 230 240
INWCPRCGTA VSDLEVDHKD LAGHIWHLRY PLEDGSGFVT VATTRPETMQ GDTAVAIHPD
250 260 270 280 290 300
DTRYAGMVGK NVVLPIMNRR IPVIADEAVD MAFGTGAVKV TPAHDPNDFE MGLRHNLPMI
310 320 330 340 350 360
TIQNRDTTMN ENAGPCSGMT AKACREYVVS EMKSLGLLLR IEDYIHSVGH CQRCSAVIEP
370 380 390 400 410 420
MVSKQWFVKM EPLAKPALEA VNSGRIQILP ERFNKVYQNW MENIRDWCIS RQLWWGHRIP
430 440 450 460 470 480
VWYCPCGEMI VAKVDPTVCP KCGGTELEQD PDVLDTWFSS GLWPHSTLGW PDQTEDLKRF
490 500 510 520 530 540
YPGTVMETAY DIIFFWVARM IVMGMEDMNE VPFRTVYLHG LIRDDKGEKM SKTKGNVIDP
550 560 570 580 590 600
LKVIDQYGTD ALRFAVTFGT SPGNDSKLGQ TKLEAARNFA NKLWNASRFV IMNLGEAKEL
610 620 630 640 650 660
TPEAELPLED RWIISRMNRV TADVTRLMEE FQFGEAQRVL QDFIWGEFCD WYIELAKVRL
670 680 690 700 710 720
RDEASVSPRP VLVRVLSSIL RLLHPYMPFI TEELWSYLRP YLPESLRETD IIVAPYPAAD
730 740 750 760 770 780
KTCFDEQAES VMGSLVEIVR SLRNLRAEHN VEISRYIQAN IYAGDMASVL GNYLGAVETL
790 800 810 820 830 840
SRARPVNILP GHYSGASTAT EVVLVLTGIE VVVPMSTMVD LEVEAKRVKA EISELEIQIE
850 860 870
RLSTRLSDEQ FLAKAPQAVV DKERIKLEGY IEKVSRLKSA