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 B3GYI3

Entry ID Method Resolution Chain Position Source
AF-B3GYI3-F1 Predicted AlphaFoldDB

No variants for B3GYI3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B3GYI3

No associated diseases with B3GYI3

5 regional properties for B3GYI3

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 48 - 59 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 20 - 637 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 677 - 825 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 889 - 949 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 636 - 767 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
MTQNLQMADR FDSSAVEQAL YKHWEEQGYF KPTENPSLPS YCIAIPPPNV TGSLHMGHAF
70 80 90 100 110 120
QQTLMDTLIR FNRMEGNNTL WQTGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFINKI
130 140 150 160 170 180
WDWKAYSGGT ISQQMRRLGN SIDWDREHFT MDEGLSNAVK EVFVRLHEEG LIYRGKRLVN
190 200 210 220 230 240
WDPKLHTAIS DLEVENKESK GSLWHFRYPL ANGAKTADGK DYLVVATTRP ETVLGDTAVA
250 260 270 280 290 300
VHPEDERYQS LIGKTVVLPL ANREIPIVAD EYVDREFGTG VVKITPAHDF NDYEVGKRHG
310 320 330 340 350 360
LPMVNVMTMN ADIRAEAEII GTDGKPLTTY EAKIPADYQG LERFAARKKV VADFEALGLL
370 380 390 400 410 420
DEIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLAEVAT KAVEDGEIQF VPKQYENLYF
430 440 450 460 470 480
SWMRDIQDWC ISRQLWWGHR IPAWYDEAGN VYVARSEEEV RQKHNLPADL ALRQDEDVLD
490 500 510 520 530 540
TWFSSGLWTF STLGWPEQTK ELKMFHPTDV LITGFDIIFF WVARMIMFTM HFVKDENGKP
550 560 570 580 590 600
QVPFKTVYVT GLIRDEQGQK MSKSKGNVLD PIDMIDGISL EDLLEKRTGN MMQPQLAEKI
610 620 630 640 650 660
AKATRKEFEN GIAAHGTDAL RFTLAALASN GRDINWDMKR LEGYRNFCNK LWNASRFVLT
670 680 690 700 710 720
NDKLDLSAGE VEYSLADRWI ESKFNRTVGE FREALSQYRF DLAANAIYDF TWNEFCDWYL
730 740 750 760 770 780
ELTKPVFANG TEAQKRGASQ TLVRVLEKLL RLAHPIMPFI TEEIWQKVKG FAGIDADTIM
790 800 810 820 830 840
LQPFPKVVKS ELDESAEMQI GWIKELIIAV RNIRAESNIA PSKGLEFLVR NVSDEQRKIL
850 860 870 880 890 900
AENDRLLKAM AKLDSVQVLS ADENAPLSVA KLVGNVEVLI PMAGFINKEA ELARLTKEIE
910 920 930 940 950
KMRGEITRIE NKLGNEAFVA KAPEAVIAKE REKMQEYQNG LEKLQTQYQA IENL