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 Q2JV13

Entry ID Method Resolution Chain Position Source
AF-Q2JV13-F1 Predicted AlphaFoldDB

No variants for Q2JV13

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2JV13

No associated diseases with Q2JV13

6 regional properties for Q2JV13

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 173 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 426 - 585 IPR002300-2
domain Aminoacyl-tRNA synthetase, class Ia 625 - 664 IPR002300-3
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 717 - 833 IPR013155
domain Leucyl-tRNA synthetase, editing domain 223 - 400 IPR025709

Functions

Description
EC Number 6.1.1.4 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.
leucine-tRNA ligase activity Catalysis of the reaction: L-leucine + ATP + tRNA(Leu) = AMP + diphosphate + 2 H(+) + Leu-tRNA(Leu).

1 GO annotations of biological process

Name Definition
leucyl-tRNA aminoacylation The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-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
MDARYNPPAI ESKWQAHWRE LGLDRTPELT AESRKFYALS MFPYPSGSLH MGHVRNYTIT
70 80 90 100 110 120
DVIARHKRMQ GYAVLHPMGW DAFGLPAENA AIDRGIPPAK WTYQNIAQMR DQLQRLGLSY
130 140 150 160 170 180
DWEREITTCA PDYYKWTQWL FLQFFKAGLA YQKEAPVNWD PVDQTVLANE QVDAEGRSWR
190 200 210 220 230 240
SGALVEKRLL KQWFLKITAY ADQLLADLEK LSGWPERVLT MQENWIGQSV GARVVFKTET
250 260 270 280 290 300
GEELPVFTTR PDTLWGATFM VLAPEHPLVE KLTTPEQEVA VKAYRAEAAA RSEIERSAED
310 320 330 340 350 360
REKTGVWTGS YAINPVNQER IPIWIADYVL MGYGTGAIMA VPAHDQRDFE FARQFGLPIK
370 380 390 400 410 420
LVVQPPQGGV TSAEDLQAAW TGEGVLINSG PLNGIPVGKG PGQSVERAIA WLEEQGLGER
430 440 450 460 470 480
QVNYRLRDWL ISRQRYWGCP IPIIHCPHCG IVPVPEEDLP VLLPEDVELT GRGGSPLAQL
490 500 510 520 530 540
EDWVKVKCPA CGADARRETD TMDTFICSSW YFLRFSDPRN DREIFRKDLV NAWLPVDQYV
550 560 570 580 590 600
GGIEHAILHL LYSRFFTKVL RDLGLLNFDE PFSRLLTQGM VQARTYYNPN KSGKDRWIPT
610 620 630 640 650 660
ALVKDPNDPR DPETGEPLQV IYATMSKSKG NGVDPEEVLA NYGADTARMF ILFKAPPEKD
670 680 690 700 710 720
LEWDDADVEG QFRFLNRVWR QVYEFVVRGS GTESLQGKAA ELLQAKVEAG SLTKAERDLR
730 740 750 760 770 780
RAVHTAIKEV SEDLEEYQFN TAIAGLMKLS NALAEAEIPD SPVYAEGIRT LVLLLAPFAP
790 800 810 820 830 840
HMAEELWQAL GGTDSVHRQA WPTYDPAALV ADTVTIVVQV NGKLRGSFEA PADVTPQEQE
850 860 870
RLALQSEAAQ RYLQGMTPKR VIVVPKKLVN LVV