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 Q488M6

Entry ID Method Resolution Chain Position Source
AF-Q488M6-F1 Predicted AlphaFoldDB

No variants for Q488M6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q488M6

No associated diseases with Q488M6

5 regional properties for Q488M6

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 57 - 68 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 31 - 646 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 694 - 846 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 908 - 966 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 645 - 784 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
MLQQNNEQLL NLLPDKMMEK TFNPTDIEQS LYTSWEEQGY FSPTGEGDSY SIAIPPPNVT
70 80 90 100 110 120
GSLHMGHAFQ QTIMDTLIRY QRMQGKNTLW QTGCDHAGIA TQMVVERKIA AEEDKTRHDY
130 140 150 160 170 180
GREGFIDKIW EWKEESGGTI GKQMRRLGNS IDWSRERFTM DDGMSEAVQE VFVRLFEDDL
190 200 210 220 230 240
IYRGKRLVNW DPKFHTAISD LEVENKDKKG HMWHLRYPLA NGAKTAEGLD YLVVATTRPE
250 260 270 280 290 300
TMLGDTGVAV NPEDPRYKDL IGKQVLLPLV NRLIPIVGDD HADMEKGTGC VKITPGHDFN
310 320 330 340 350 360
DNEVGKRHAL PQINILDKDA AILATAEVYD TKGEVCNAYD TGLPSEFAGM DRFVARKAIV
370 380 390 400 410 420
AKFDELGLLV EVKDHDLVAP YGDRSGVIIE PLLTDQWYVR VEKLAGPAVD AVKDGQIEFV
430 440 450 460 470 480
PKQYENMYFS WMNNIQDWCI SRQLWWGHRI PAWYDENEKV YVGRTEEEVR ANNDIAADMK
490 500 510 520 530 540
LRQDDDVLDT WFSSALWTFS TLGWPKDTED LKTFHPTDVL VTGFDIIFFW VARMIMMTMH
550 560 570 580 590 600
FNKDENGKAQ IPFKKIYMTG LIRDENGDKM SKSKGNVVDP LDMIDGISLE DLLQKRTGNM
610 620 630 640 650 660
MQPKLAKKIE KLTRKEYPEG IEAHGTDALR FTLTSVATTG RDISWDMKRL EGYRNFTNKL
670 680 690 700 710 720
WNASRYVMMN TEEFDCGQSS PEGKAGDMEL SLADRWIIGQ FEQTVKTVHE AFDTYRFDLA
730 740 750 760 770 780
SQALYEFTWN QFCDWYLELT KPVLFKENEA QQRGTRHTLV NVLEALLRLM HPIMPFITET
790 800 810 820 830 840
IWQRVQPLSD FSKNGDSIMV QAFPQFDESK CDQQAIDDLE WVKQFIIAIR NIRGEMDISP
850 860 870 880 890 900
SKELPVLLKN VNDNDQRRLD ENEQFLSSLA KLESITVLAD DEQGPASASA VVGDLSVLIP
910 920 930 940 950 960
MAGLIDKEAE LARLDKAIEK LEKEAGRVRG KLGNENFVSK APAAVIEKEQ AKLADAESTL
970
AKILEQKIQI AAL