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 Q8SS27

Entry ID Method Resolution Chain Position Source
AF-Q8SS27-F1 Predicted AlphaFoldDB

No variants for Q8SS27

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8SS27

No associated diseases with Q8SS27

4 regional properties for Q8SS27

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 84 - 95 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 57 - 679 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 741 - 861 IPR013155
domain Valyl tRNA synthetase, anticodon-binding domain 678 - 823 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
MDSSKEALKE RKKMAKDEKK RQKLEKFLAK KTLEIGVSKP RKEYRKEGYD PLQVEGKWYK
70 80 90 100 110 120
LWEEQGLFKP VEGGARYVVP IPPPNVTGSL HIGHAMMVSI QDAVCRYKRM CGYEVLYIPG
130 140 150 160 170 180
TDHAGIATQN VVSKQLAREG IVVDREGFLK KAWEWKDRHG SRIYEQLKRL GTSVDFGRER
190 200 210 220 230 240
FTLDPGMSRA VADAFVKLYE KGLIYREPKI VNWCSRLLTT ISDLEVNHEE VMPNTYLQVD
250 260 270 280 290 300
GGKYEFGVIY HFKYPITADK GFSGDHLSLP TIEVATTRPE TILGDTAVCV NGRDCRFSPE
310 320 330 340 350 360
GIKEMLGDVP HGCRIYGVNP LTRDVIPVIF DDYADMSFGT GVVKITPAHD ANDFEVSKRH
370 380 390 400 410 420
GLPCKVVFDE QNRVVVEGEF KGLKRFEARK AVVSKLRDVG LFVSKKGHPQ VIPRCSRSDD
430 440 450 460 470 480
VIEPIIKSQW WLNCKEMARK AIEAVEDGRI SILPEGAEKQ WYKWLGNIRD WCLSRQLWWG
490 500 510 520 530 540
HRVPAYKAPS GKWYVGRTKE DAFLKMRSEC MGSDCDLSEL EQDEDVLDTW FSSGLWPFAT
550 560 570 580 590 600
LGWPEETEDF LKYYPNTLLE TGSDILFFWV ARMVMLGLEL TGKVPFSQVL LHGIVRDAHG
610 620 630 640 650 660
RKMSKSLGNV IDPIFVIDGC SLEKLISTMR SGNLDEREVK RAEAVLRQDF PNGISRCGAD
670 680 690 700 710 720
ALRFALLSYT SGMKDINLDV LRVEGYRRFC NKIWNAHKFV KTMVDELAGK NGNGPVCKDD
730 740 750 760 770 780
YGKYIVSSAE LPGPSEEGPV EWILRRRNET VEEIRRTLDS FNFMGATQAI HQFFIYDLCD
790 800 810 820 830 840
VFIEVVKKSK NEKYIRVLFR VFIDSMKMLH PFMPFITEEV FSNYFNGSIS VSPYPETDGS
850 860 870 880 890 900
EHESKFSVTL QITRHIRAKA ESNGWSKAVV EIAPGGDVNH ADLRFIRSLC RKIVELKIIS
910 920
DAEDGPYEKV GGSRVLVRQT E