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 B8CXR8

Entry ID Method Resolution Chain Position Source
AF-B8CXR8-F1 Predicted AlphaFoldDB

No variants for B8CXR8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B8CXR8

No associated diseases with B8CXR8

5 regional properties for B8CXR8

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 424 - 625 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 668 - 792 IPR013155
domain Methionyl/Leucyl tRNA synthetase 37 - 190 IPR015413
domain Leucyl-tRNA synthetase, editing domain 222 - 410 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
MKGYYNFADI EKKWQDKWEK DGLYKTQEET DKDNYYVLEM FPYPSGNLHM GHVRVYSIGD
70 80 90 100 110 120
VIARFKRMNG YNVLHPMGWD AFGLPAENAA IKHGNIHPQD WTWDNIKNMK KQMKSLGLSY
130 140 150 160 170 180
DWDREVTTAK EDYYKWTQWF FVKMFKKGLA YKKKAAVNWC PGCETVLANE QVVNNACERC
190 200 210 220 230 240
GTEVEEKELE QWFFKITNYA ERLLEDHKLL QNWPEKVKIM QRNWIGRSEG MRIKFPVKGS
250 260 270 280 290 300
SEEIEVFTTR PDTIFGATYM VLAPEHPLVE KLISGTEKEK EVRQFIDRVK KQKEMERTSP
310 320 330 340 350 360
ESEKEGLFTG AYAINPMTGE EIPIMIANYV LMGYGTGAIM AVPAHDQRDF DFARKYDLPI
370 380 390 400 410 420
RVVIQPEERE EELKDTDLNE AYEGSGHLIN SDKYNGLTVK EAFDVMAEDM EKEGIGKREV
430 440 450 460 470 480
NYRLRDWLIS RQRYWGTPIP IVYCEKCGTV PVPEEELPVV LPRDVEFSPT GESPLAKVDE
490 500 510 520 530 540
FVNTTCPVCG GKARRETDTM DTFVDSSWYF LRYTDPKNDK LPFSKENAKK WFPVDQYIGG
550 560 570 580 590 600
IEHAILHLLY ARFFTKVIYD MDMIDSVEPF TNWLAQGMVL KDGAKMSKSK GNVVDPEDIL
610 620 630 640 650 660
DRFGADTARL FILFAAPPEK DLEWSDRGVE GAERFLNRVW RLVADNIKEI KNTDQASLDV
670 680 690 700 710 720
NSFNKNEKDL YRNLHVTIKR VTEDIGERLN FNTAISAIME LTNATYQYLN GVEKVNYTLI
730 740 750 760 770 780
KDIIEKMLLI LAPFAPHMTE ELWSELGNDE SIHIQKWPGY EEKALKKDEV TIVVQVNGKV
790 800 810 820
RDKLQVSADI DEDKLKEQVL ELPRIQKYTE GKEIVKTIII PKKLVNIVVK