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 C4V924

Entry ID Method Resolution Chain Position Source
AF-C4V924-F1 Predicted AlphaFoldDB

No variants for C4V924

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C4V924

No associated diseases with C4V924

4 regional properties for C4V924

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 82 - 93 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 56 - 663 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 717 - 843 IPR013155
domain Valyl tRNA synthetase, anticodon-binding domain 662 - 799 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
MTLKMDRKAL KEEKKKQKLE KFLNKKTTQS KISKAPKPAK NKSSSGYDPM PVEQKWNNYW
70 80 90 100 110 120
LSNNLFEPQE RSNKFVMCMP PPNITGSLHI GHSMMIAIQD AICRYMRLIN YEVLYLPGTD
130 140 150 160 170 180
HAGIATQTVV MKQLEKEKKT YNRESFLEAT WKWKENYGSR ILDQFKRLGT SADFSRQKFT
190 200 210 220 230 240
MDAGMNKAVT EAFCSLYEKG LIYRDNKIVN WCCKLQTTLS DIEIDYLSVG KNTILKIDGR
250 260 270 280 290 300
DYEFGVIYVF KYPVKFVKDG YESEGHIEVA TTRPETILGD VALCANPKDA RYTKYDKIIP
310 320 330 340 350 360
RNPITEEELS FVFDEAAEMD LESGVLKITP AHDPIDFEIG KKNNLKNIKI FDNQNKIIIE
370 380 390 400 410 420
GNYYKLKRLD ARDLVVQTLK NKNLFVEKKP YEQVLPMCSR SSDLLEPVIK EQWWCSCSEM
430 440 450 460 470 480
AKKAIDAVKT EQIKIYPEES KDDWYRWFEN PRDWCLSRQL WWGHRIPAYK TPDGVWTIAR
490 500 510 520 530 540
NKEQAIQSYK KNNPLNVHYQ ESDFVQDEDV LDTWFSSGLW PFATLGWPNK NQDLDKYFPT
550 560 570 580 590 600
SLLETGKDIL FFWVGRMVMM SLELTGKVPF KKVLLHGIVR DAYGRKMSKS LGNVIDPIHV
610 620 630 640 650 660
IDGASIETLL DALKLGNLTK ENLINAESAV KKDFINGITV CGADALRFTL LSYMNGINDI
670 680 690 700 710 720
KLDIERVKGN RKFCNKIWNA ALFVKKIVDE IISSDSLSYQ DLLNLDLSNE DDKLLVWLIQ
730 740 750 760 770 780
ERNKVISTTH KAFKEYKFMS AVQSIHQFFL YDFCDVYIEI VKKIKTKKYI QACFMVLIDS
790 800 810 820 830 840
IKIFSPYMPF ITEEIYSQFF DNSLMYTSYP EIIHNKFSTN FKSTLSKIKA IRADIEKYGK
850 860 870 880
EKVDVILDGC ECFDKIDIQF ISILIPNINT IKFGEGYEVK KVN