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 Q4A755

Entry ID Method Resolution Chain Position Source
AF-Q4A755-F1 Predicted AlphaFoldDB

No variants for Q4A755

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4A755

No associated diseases with Q4A755

5 regional properties for Q4A755

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 41 - 52 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 15 - 421 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 423 - 550 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 586 - 712 IPR013155
domain Valyl tRNA synthetase, anticodon-binding domain 550 - 667 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
MKNKYDFKLV EEKRNEKWQK KGFFIAPKQT KKPFSIISPP PNVTGQLHLG HSWNAFIQDS
70 80 90 100 110 120
LVRYHKLQGF DVLLLPSVDH AGIATQVKVE EDLAKKGIKK SDLKREEFIK KCYHWKEKQY
130 140 150 160 170 180
LKIKEQWDKL GICYDFSKER FTLDQDAQIA VSDFFIKLWE KNLIYRGQKA INWDIKLQTA
190 200 210 220 230 240
ISNIEVINKP VEQKMYYLKY FLENSNEFLT VATTRIETIS SDVALAINPK DKRYLHLVGK
250 260 270 280 290 300
KVVHPLTKKL IIIIADSNVS SDFGSGIMKV SAHSILDFEI MEKHNLESKD CIDNYGNLNH
310 320 330 340 350 360
EVPEFQGQNR FFARDLIAKK LEKEGFLAKI ETVISNVGFS QRSDEIVEIL KKPQWFVKMD
370 380 390 400 410 420
ELAKSLISHL NSKDKIKFYP KNFEKNLRKW FEKIHDWTIS RQLWWGHRIP VWCKNDEFKV
430 440 450 460 470 480
QIDSPGQGWI QDEDVLDTWF SSGISAFAFL GWPQNFDLIK SYFPTSLLVT GWDILFFWVA
490 500 510 520 530 540
RMYFSSLFIM KQKPFEKVLL HGLIRDEIGR KMSKSLGNGL DPMEIIEKYG SDTLRQALIF
550 560 570 580 590 600
NSSPGKDIKF NIEKLNTAWN LNNKIWNIAK YIADLDTFFA KPDLIDLWME NKIYILKRQI
610 620 630 640 650 660
VKNIKKYNFS VIGTEINNFI YGDFSSRYIE LIKTRKNGFY ARKLLRKVLI ILHPFLPFLT
670 680 690 700 710 720
DFLMEKIFKM EILEQKMPRI RQFKENQKVE NILEIIDNLR TYREKFQISK KIILEYCIIN
730 740 750 760 770 780
DKFSNAEIDI INKLTFGKWL ENKELVIKTK NFEIAIKVPE ELKKEQKGRE LKEIQFLKSE
790 800 810 820
ILRAEKILTN KGFLEKAPRE KIDLERTKLE KLKEKLAFYE KK