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 A5V1W3

Entry ID Method Resolution Chain Position Source
AF-A5V1W3-F1 Predicted AlphaFoldDB

No variants for A5V1W3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5V1W3

No associated diseases with A5V1W3

5 regional properties for A5V1W3

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 49 - 60 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 21 - 179 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 443 - 599 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 744 - 863 IPR013155
domain Leucyl-tRNA synthetase, editing domain 229 - 421 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
MSETGAKRRM DRFDPSIEPK WREFWAREGI FKAGRRAGAP RRYILEMFPY PSGDLHIGHL
70 80 90 100 110 120
KNYVIGDALT RYYVIRGYDV LHPFGWDAFG LPAENAAIKY GRHPREWTYS NIAESKKSLE
130 140 150 160 170 180
IAGIMYDWSR EVTTCNPDYY RWNQWLFLLL YRKGLAYRAK ATVNWDPVDQ TVLANEQVDA
190 200 210 220 230 240
EGRSWRSGAK VEKRELEQWF FRITAYAERL LNDLDKLDRW PENVKTMQRN WIGRSEGAEV
250 260 270 280 290 300
TFLALPPGAD LYAPPPPDAE PLVVFTTRPD TLWGATFMVL APEHPLAPKL TAPERRAEVE
310 320 330 340 350 360
AYIARARMES EIERTSATRE KSGVFLGSYA INPVNDERIP IWIADYVLMG YGTGAIMAVP
370 380 390 400 410 420
AHDQRDFEFA RQFGLPVRVV VQPPGETLDG DTMTEAWPGD GVMVNSGPIN GIPVGKGEGQ
430 440 450 460 470 480
SVKAAIAWLE AQGKGKGTVT YRLRDWLISR QRYWGTPIPM LHLPDGTIKP VPEDQLPVLL
490 500 510 520 530 540
PEVQDYLPKG KSPLAAAEHW VNTIDPETGQ PARRDTDTMD TFVDSSWYFL RFCDAQNDRE
550 560 570 580 590 600
IFSREAARQW MPVDQYIGGV EHAILHLLYA RFITKVLYDE GLVPEDEPFK ALFTQGMVQR
610 620 630 640 650 660
RVRTPLDIVA PGMVRFPEEL RRKLELPAEA QTVDQARALL KERGYTLEEE SDGGLTAVSG
670 680 690 700 710 720
PVTMSKSAGN GIPVGPFVRQ YGSDVARIVV LFAAPPENSM EWTDEGVAGA QRFLNRIVAL
730 740 750 760 770 780
FGPDRDEIAA MVRSGNGAAP EGEDRALYRK LHETIRKVTL DTEQFRFNTA IAALMELLNE
790 800 810 820 830 840
ASRYRAEVGR VTPVFAQTAA TFARLLSPFA PHLAEEVHSW CGGTGSVYDA GWPEWDESAL
850 860 870 880 890 900
VLDEVEIVLQ VNGKLRGKIM APAGADEEQL REWALTNPRV LSFVGDKTVR KVIVVPGKLV
NVVV