Q4JWU8

PR
Gene name
valS
Protein name
Valine--tRNA ligase
Names
Valyl-tRNA synthetase, ValRS
Species
Corynebacterium jeikeium (strain K411)
KEGG Pathway
cjk:jk0550
EC number
6.1.1.9: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-67 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q4JWU8

Entry ID Method Resolution Chain Position Source
AF-Q4JWU8-F1 Predicted AlphaFoldDB

No variants for Q4JWU8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4JWU8

No associated diseases with Q4JWU8

6 regional properties for Q4JWU8

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 75 - 86 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 47 - 459 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 472 - 605 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 649 - 809 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 865 - 929 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 609 - 747 IPR033705

Functions

Description
EC Number 6.1.1.9 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.
valine-tRNA ligase activity Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
valyl-tRNA aminoacylation The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-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
MPCLARLLDL ADVSDSSSKA NGSNPIGADR SAQLPAAWDP AAVEENLYQG WVDSGYFKAD
70 80 90 100 110 120
PSSDKPPFSI VLPPPNVTGQ LHMGHALDHT LMDAMARRKR MQGFEVLWLP GSDHAGIATQ
130 140 150 160 170 180
TKVEANLKET EGKDRFDYGR DAFVGKVWEW KDRYGGVIQR QMRAIGDSVD WSRERFTLDD
190 200 210 220 230 240
GLSRAVQTMF KELFDAGLIY RANRMVNWSP VLQTAISDIE VVYSDDEGEL VSIRYGSLED
250 260 270 280 290 300
SEPHVVVATT RVETMLGDVA VAVHPEDERY TDLVGKSLPH PFLPDRQMIV VADDYVDPEF
310 320 330 340 350 360
GTGAVKITPA HDPNDFAMGQ RHDLPMPVIM DETGHIANTG TEFDGMERYE AREKIRLALE
370 380 390 400 410 420
EQGRIVARKF PYVHSVGHSE RSKEAVEPRL SEQWFVKVEE LAKMSGDAIR SGDSVIHPSS
430 440 450 460 470 480
QEPRWFDWVD DMHDWCISRQ LWWGHRIPIW YGPNGEIVCC GPDDEAPTGE GWYQDEDVLD
490 500 510 520 530 540
TWFSSALWPF STMGWPEKTP ELEKFYPTSV LVTGYDILFF WVARMMMFAT FASKHTPEIL
550 560 570 580 590 600
GTGKDGRPQI PFNDIFLHGL VRDEHGRKMS KSLGNGIDPM DWVRDYGADA LRFTLARGAN
610 620 630 640 650 660
PGSDLPVGED AAQSSRNFAT KLYNATKFAL MNGARVGELP ARETLTDADR WILDRLEEVR
670 680 690 700 710 720
QLVDDALDRY EFSLANENLY RFAWGEFCDW YLEIAKVQIP RDWDSATEEQ VQRGIRTQIV
730 740 750 760 770 780
LGRVLDSVLR LLHPAMPFVT ETLWKALTDG EEGYSESLVT ADWPTADLTN GGAQTDADAV
790 800 810 820 830 840
RRMADVDKLV TELRRFRSDQ GVKPSQKVPA KLDFAAADLA NFEEAVRSLV RLETPEEDFA
850 860 870 880 890 900
ETASIEVRLS QATIAVQLDT SGTVDVAAER KRLEKDLAAA QKELDNAAKK LGNENFLAKA
910 920 930
PEKVVEGIRE RQRVAQEEFE RITARLEGLP KA