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 Q891R5

Entry ID Method Resolution Chain Position Source
AF-Q891R5-F1 Predicted AlphaFoldDB

No variants for Q891R5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q891R5

No associated diseases with Q891R5

5 regional properties for Q891R5

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 48 - 59 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 20 - 565 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 610 - 758 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 815 - 880 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 566 - 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
MNDNINIAKT YDPKEFEERI YKMWEEGEYF TPKVDKDKKP YTIVMPPPNI TGKLHLGHAL
70 80 90 100 110 120
DNSMQDFLIR VKRMQGYSTL WLPGQDHASI ATEVKVENEL LKTGLKKKEM GREAFLERVW
130 140 150 160 170 180
EWSEEYRGRI RDQLKKLGSS ADFTRESFTM DDNLDKAVRA VFVKLYEEGL IYKGNRIVNW
190 200 210 220 230 240
CPKCMTALSD AEIEYEENYG NFWHVKYPLV DSEEYLEIAT TRPETMLGDT AVAVNPNDER
250 260 270 280 290 300
YKHLIGKKLM LPLVNREIPI VADDYVDVEF GTGAVKITPA HDPNDYEVGK RHDLEEIIIM
310 320 330 340 350 360
NENGTINELG GKYSGMDRYE ARKAIVEDLK KEGFLVKVKE HIHNVSCHDR CNTIIEPMIS
370 380 390 400 410 420
KQWYVKMKEL AKPAIEVVKS GEIKFVPERF DKTYFNWMEN IQDWCISRQL WWGHRIPVWY
430 440 450 460 470 480
CKDCGETIVS LEEAKKCSKC SSENLIQDED VLDTWFSSAL WPFSTLGWPD KTEDLEYFYP
490 500 510 520 530 540
TDVLATGYDI IFFWVARMIF SGLHNMKEIP FKTVLIHGIV RDSEGKKMSK SLGNGVDPLE
550 560 570 580 590 600
VIDKYGADAL RFMLITGNAP GNDIRFYEER VESARNFANK IWNASRYVMM NLDKNLMEKY
610 620 630 640 650 660
KDCKDYNIAD TWILSRLNEV IKEVTDNIEK FELGMASQKV YDFMWNEFCD WYIELSKPVL
670 680 690 700 710 720
YGEDEKAKGV TFNVLFNVLT SGLKLLHPIM PFITEEIFIN IQEEEKTITT SKWPEFKEEL
730 740 750 760 770 780
KNEEVEKKMS HVIEAIKAIR NVRIEMDVPP SRKAKIMIYA LDGIDAFKDG KIYFEKLASA
790 800 810 820 830 840
SEVEFLNSKE EAPENAVSAV TKGAEIYIPL FDLVDLEKEM ERLNKEREKL EKEIERVDKK
850 860 870
LSNENFVKKA PEAVVNEEKA KGEKYKEMLE AVLERIKSLK