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 B0C1R1

Entry ID Method Resolution Chain Position Source
AF-B0C1R1-F1 Predicted AlphaFoldDB

No variants for B0C1R1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0C1R1

No associated diseases with B0C1R1

5 regional properties for B0C1R1

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 420 - 577 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 696 - 814 IPR013155
domain Methionyl/Leucyl tRNA synthetase 40 - 172 IPR015413
domain Leucyl-tRNA synthetase, editing domain 223 - 406 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
MESRYNPTEI EPKWQASWAK QGLDATPEDT SKPKFYALSM FPYPSGSLHV GHTRNYVITD
70 80 90 100 110 120
VIARLKRMQG YRVLQPMGWD AFGLPAENAA IARGIHPAEW TYANMAQMKK QLEPLGLSID
130 140 150 160 170 180
WSREIATCSP DYYRWTQWIF LQFLDMGLAY QKEAAVNWDP VDQTVLANEQ VDNEGRSWRS
190 200 210 220 230 240
GAKVERKLLR QWFLKITDYA EELLTDLDKL TGWPERVKTM QANWIGKSVG AYLEFPIVGM
250 260 270 280 290 300
DEKVAVFTTR PDTVYGVTYV VLAPEHPLTP QVTSKAQKKA VDKFIEAVGA ESEMDRTAED
310 320 330 340 350 360
KPKKGIPTGG KAINPFTGEE IPIWIADYVL YEYGTGAVMG VPAHDTRDFV FAQQNKLPIQ
370 380 390 400 410 420
TVIVPEGGDA ETPLEAAYTE PGLMVNSGEF DGKVSTEGKQ AIIAKAETKG WGKARVQYRL
430 440 450 460 470 480
RDWLISRQRY WGVPIPVIHC PNCGAVPVPE ADLPVELPED VEFSAQGGSP LAKLESWVNV
490 500 510 520 530 540
ACPNCGADAK RETDTMDTFI DSSWYFLRYP DAKNDKAVFD SAKTNDWLPV DQYVGGIEHA
550 560 570 580 590 600
ILHLLYSRFF TKVMRDRKLL NFDEPFKKLL TQGMVQALTY KNPETGQYIA PINVDADDPK
610 620 630 640 650 660
DPETGAPLEA FYEKMSKSKY NGVPPEEVTN KYGADTARLF TLFKAPPEKD LEWEGADVEG
670 680 690 700 710 720
QFRFLNRVWR LVSEHAAQAK GKKAKVNKAK LSKTEKELRR SIHIAIKETS EDLDGDYQFN
730 740 750 760 770 780
TAVSELMKLS NALSDSKEKA SPVYAEGVET LLLLLTPFAP HISEELWENL GHSESILGQT
790 800 810 820 830 840
WPQVDEEALV ADEITLVIQI MGKTRGTIQV PAGSSREDLE QLARESEVAQ RYIAGKEVKK
850
VIVVPGKLVN FVVPK