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 Q5M5J8

Entry ID Method Resolution Chain Position Source
AF-Q5M5J8-F1 Predicted AlphaFoldDB

No variants for Q5M5J8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5M5J8

No associated diseases with Q5M5J8

6 regional properties for Q5M5J8

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 46 - 57 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 18 - 430 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 435 - 560 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 610 - 755 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 814 - 878 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 559 - 698 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
MSKELSPKYN PAEVEAGRYQ KWLDEDVFKP SGDKKAKPYS IVIPPPNVTG KLHLGHAWDT
70 80 90 100 110 120
TLQDIIIRQK RMQGFDTLWL PGMDHAGIAT QAKVEARLAE SGISRYDLGR EKFLDKVWEW
130 140 150 160 170 180
KDEYAATIKE QWGKMGLSVD YSRERFTLDE GLSKAVRKVF VELYKKGWIY RGEFIINWDP
190 200 210 220 230 240
KARTALSDIE VIHKDVEGAF YHMNYMLEDG SRALEVATTR PETMFGDTAV AVNPNDDRYK
250 260 270 280 290 300
DLIGKNVILP ILNKPIPIVG DEHADPEFGT GVVKITPAHD PNDFLVGQRH NLPQVNVMND
310 320 330 340 350 360
DGTMNELAGE FNGMDRFEAR KAIVKKLEEI GALVEIEKMT HSVGHSERTG VPVEPRLSTQ
370 380 390 400 410 420
WFVKMDQLAK NAIANQDTDD KVDFYPPRFN DTFLQWMENV HDWVISRQLW WGHQIPAWYN
430 440 450 460 470 480
AEGEIYVGEE APEGDGWKQD EDVLDTWFSS ALWPFSTMGW PDVDSEDFKR YFPTSTLVTG
490 500 510 520 530 540
YDIIFFWVSR MIFQSLEFTG RQPFKNVLIH GLIRDEQGRK MSKSLGNGID PMDVIEKYGA
550 560 570 580 590 600
DALRWFLSNG SAPGQDVRFS YEKMDASWNF INKIWNISRY ILMNNEGLTL DVARENVAKV
610 620 630 640 650 660
AAGQAGNVTD RWILHNLNET IRKVTENFDK FEFGVAGHIL YNFIWDEFAD WYVELTKEVL
670 680 690 700 710 720
YSDNEDEKVI TRSVLLYTLD QILRLLHPIM PFVTEEIFGQ ISEGSIVTAE YPVARPEFEN
730 740 750 760 770 780
EEAAAGVEAL KDVIRSVRNS RAEVNVAPSK PITILIKTSD SKLDAFFNDN INYIKRFTNP
790 800 810 820 830 840
EHLEIAADVE VPDLVMSSII TGAEIYLPLA DLLNVEEELA RLEKELAKWQ KELDMVGKKL
850 860 870 880
SNERFVANAK PEVVQKERDK QKDYQAKYDA IVVRIDEMKK LVK