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 Q9YD97

Entry ID Method Resolution Chain Position Source
AF-Q9YD97-F1 Predicted AlphaFoldDB

No variants for Q9YD97

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9YD97

No associated diseases with Q9YD97

3 regional properties for Q9YD97

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class Ia 10 - 325 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 397 - 663 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 713 - 831 IPR013155

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
MERLKAVEEK WQERWREARL FEADPQPGRR KFFITFPYPY VNAYPHLGSA FTILRVDIMA
70 80 90 100 110 120
RYKRMRGYNV LFPQGWHATG GPIVSSALRV REGDPRIIKT LRDMGIPEED IPRFRDPRYW
130 140 150 160 170 180
VEFFTKAWRR DLERYGMSID WRREFYTTSL NPAYSRFIEW QYLKLREKGF VGKGRHPVVW
190 200 210 220 230 240
CPKEQKVVGD HDRPDEYAGI SPQEAVIIKF RGRDGLVYPA LTYRPETVFG VTNLWVHPDA
250 260 270 280 290 300
TYLVAEVDGE ERWIIGEQAA RELADQGHRV VILERIEGRR LLGRIVVNPA DGREVPVLPA
310 320 330 340 350 360
SFVRPDLGTG VVMSVPAHAP YDYVALMELK RRPETLREYG LEPGVVESLE PIQLIAVPRA
370 380 390 400 410 420
EGLLVVEEVR RRGVESQMDR EKLDEATREV YAREFYEGIM LETTGRFSGL KVAEAKEKVV
430 440 450 460 470 480
EWLEERGAAL RIYTLPQEVY CRCGARTHVK IVEDQWFLLY SKPEWKALAR EAVARMEFLP
490 500 510 520 530 540
GHVRRDFEAI IEALRDWAFT HKGELGTPLP WDREWVIESL SDSTIYMAYY TIAKYTQHPE
550 560 570 580 590 600
KYGVEPEMLT PEVFDYVFLG AGDPGEVSRR SGIPQGLLEE MRREFLYWYP LDMRISGKDL
610 620 630 640 650 660
IPNHLVFFIF HHTAIFPREL WPRAIGVNGW VLVAGEKMSK SKGNFILLRQ ALDWWGADAT
670 680 690 700 710 720
RWAEVLAGAD SGLDDANFEP SVADSAVSLL SQWLDFVREN YGRPARREER WVDRWFESRL
730 740 750 760 770 780
NSTIARVTRL MEEANFKTAL VEAWYKLQES YRWYLRRSGG EPREDLLRRF IEVQTLLIAP
790 800 810 820 830 840
FAPHTAEEAW EAMGREGFAS TASWPEPDES KISPEVEAAE ETVQAVLEDA REVLSLIGGA
850 860 870 880 890 900
DTLVVTVAAE WKYRAVEAVR RARERGASMK EALREAFKVE GVDKREAARL VQQLSRAPEV
910 920 930 940 950
LRRAAPRSVE LEALRDAAQL LQEELGVKVV VETEEDGGSP RRANALPGRP ALYAEKRGG