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 P49696

Entry ID Method Resolution Chain Position Source
AF-P49696-F1 Predicted AlphaFoldDB

No variants for P49696

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P49696

No associated diseases with P49696

6 regional properties for P49696

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 293 - 304 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 258 - 886 IPR002300
domain Glutathione S-transferase, C-terminal 48 - 137 IPR004046
domain Glutathione S-transferase, C-terminal-like 27 - 155 IPR010987
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 931 - 1083 IPR013155
domain Valyl tRNA synthetase, anticodon-binding domain 885 - 1027 IPR033705

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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
MATLYVSPHL DDFRSLLALV AAEYCGNAKQ QSQVWQWLSF ADNELTPVSC AVVFPLMGMT
70 80 90 100 110 120
GLDKKIQQNS RVELMRVLKV LDQALEPRTF LVGESITLAD MAVAMAVLLP FKYVLEPSDR
130 140 150 160 170 180
NVLMNVTRWF TTCINQPEFL KVLGKISLCE KMVPVTAKTS TEEAAAVHPD AAALNGPPKT
190 200 210 220 230 240
EAQLKKEAKK REKLEKFQQK KEMEAKKKMQ PVAEKKAKPE KRELGVITYD IPTPSGEKKD
250 260 270 280 290 300
VVSPLPDSYS PQYVEAAWYP WWEKQGFFKP EFGRKSIGEQ NPRGIFMMCI PPPNVTGSLH
310 320 330 340 350 360
LGHALTNAIQ DTLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLMREKG TSRHDLGREK
370 380 390 400 410 420
FIEEVWKWKN EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SYAVQEAFIR MHDEGVIYRS
430 440 450 460 470 480
KRLVNWSCSL NSAISDIEVD KNELSGRTLL PVPGYKEKVE FGVLVSFAYK VDGSDEEVVV
490 500 510 520 530 540
ATTRIETMLG DTAVAVHPSD SRYQHLKGKT VLHPFCDRKI PVVFDDFVDM SFGTGAVKIT
550 560 570 580 590 600
PAHDHNDYEV GVRHNLAFIN ILDENGFVIN VPPPFLGMKR FDARKAVLQA LKDRDQFKEI
610 620 630 640 650 660
KDNPMVVPVC SRSKDIVEPL MKPQWYVSCS DMGKQAADAV REGRLKIIPD HHSQTWFNWM
670 680 690 700 710 720
DNIRDWCISR QLWWGHRIPA YFITVSDPSV KPGEDMDGHY RVSGRTPEEA REKAAKRFNV
730 740 750 760 770 780
SPDKIALRQD EDVLDTWFSS GINPFSILGW PNETEDLNVF YPGTLLETGH DILFFWVARM
790 800 810 820 830 840
VMMGLKLTGK LPFKEVYHCA VVRDAHGRKM SKSLGNVIDP LDDHIGIALE GLHAQLMDTN
850 860 870 880 890 900
LDPLEVEKPK KVQKADYPNC IPECGTDALR FALCAYTSQG RDINLDVNRI LGYRHFCNKL
910 920 930 940 950 960
WNAVKFAMRT LGDQFVPADT SPAEREESVS DRWILSRLST AVAQCDAAFR TYDFPAITTA
970 980 990 1000 1010 1020
IYNFWLYELC DVYLESVKPV FIKAKEDGSC ERPAAVCRQT LYTCLEVGLR LLAPLMPFVT
1030 1040 1050 1060 1070 1080
EELYQRLPRR RPQSDPPSIC VTPYPDAAEF CWQCEDVDRD IDFIMGVVRT IRSLRSDYKL
1090 1100 1110 1120 1130 1140
TKTAADCYLQ CTDAATVSLV QKYSLQIQTL SYSQAIVPLM APQPAPEGCA VAIASDRCTV
1150 1160 1170 1180 1190 1200
NMMLKGLIDV EKEVPKLMGK KTDLEKQIEK LSEKISKGDY KEKVPVKVQE QDTEKLRQSQ
1210
TELEKVKEAM DNFQKMM