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 Q5XE99

Entry ID Method Resolution Chain Position Source
AF-Q5XE99-F1 Predicted AlphaFoldDB

No variants for Q5XE99

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5XE99

1 associated diseases with Q5XE99

[MIM: 125630]: Vibratory urticaria (VBU)

An autosomal dominant disorder characterized by localized hives and systemic manifestations in response to dermal vibration, with coincident degranulation of mast cells and increased histamine levels in serum. {ECO:0000269|PubMed:26841242}. Note=The disease is caused by variants affecting the gene represented in this entry.

Without disease ID
  • An autosomal dominant disorder characterized by localized hives and systemic manifestations in response to dermal vibration, with coincident degranulation of mast cells and increased histamine levels in serum. {ECO:0000269|PubMed:26841242}. Note=The disease is caused by variants affecting the gene represented in this entry.

18 regional properties for Q5XE99

Type Name Position InterPro Accession
ptm EGF-type aspartate/asparagine hydroxylation site 85 - 96 IPR000152-1
ptm EGF-type aspartate/asparagine hydroxylation site 136 - 147 IPR000152-2
ptm EGF-type aspartate/asparagine hydroxylation site 180 - 191 IPR000152-3
ptm EGF-type aspartate/asparagine hydroxylation site 229 - 240 IPR000152-4
domain GPS motif 478 - 529 IPR000203
domain EGF-like domain 28 - 66 IPR000742-1
domain EGF-like domain 67 - 118 IPR000742-2
domain EGF-like domain 119 - 162 IPR000742-3
domain EGF-like domain 163 - 211 IPR000742-4
domain EGF-like domain 212 - 260 IPR000742-5
domain EGF-like calcium-binding domain 67 - 118 IPR001881-1
domain EGF-like calcium-binding domain 119 - 162 IPR001881-2
domain EGF-like calcium-binding domain 163 - 211 IPR001881-3
domain EGF-like calcium-binding domain 212 - 260 IPR001881-4
domain GPCR, family 2-like, transmembrane domain 536 - 782 IPR017981
conserved_site GPCR, family 2, secretin-like, conserved site 770 - 785 IPR017983
conserved_site EGF-like calcium-binding, conserved site 119 - 145 IPR018097-1
conserved_site EGF-like calcium-binding, conserved site 212 - 238 IPR018097-2

Functions

Description
EC Number 6.1.1.1 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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
RNA binding Binding to an RNA molecule or a portion thereof.
tyrosine-tRNA ligase activity Catalysis of the reaction: L-tyrosine + ATP + tRNA(Tyr) = L-tyrosyl-tRNA(Tyr) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
tyrosyl-tRNA aminoacylation The process of coupling tyrosine to tyrosyl-tRNA, catalyzed by tyrosyl-tRNA synthetase. The tyrosyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tyrosine-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
MNIFEELKAR GLVFQTTDEQ ALVKALTEGQ VSYYTGYDPT ADSLHLGHLV AILTSRRLQL
70 80 90 100 110 120
AGHKPYALVG GATGLIGDPS FKDAERSLQT KETVLEWSDK IKGQLSAFLD FENGDNKAEL
130 140 150 160 170 180
VNNYDWFSQI SFIDFLRDVG KYFTVNYMMS KDSVKKRIET GISYTEFAYQ IMQGYDFYEL
190 200 210 220 230 240
NDKHNVTLQI GGSDQWGNMT AGTELLRKKA DKTGHVMTVP LITDSTGKKF GKSEGNAVWL
250 260 270 280 290 300
DADKTSPYEM YQFWLNVMDD DAVRFLKIFT FLSLDEIAEI ETQFNAARHE RLAQKTLARE
310 320 330 340 350 360
VVTLVHGEEA YKQALNITEQ LFAGNIKNLS ANELKQGLSN VPNYHVQSED SLNLVDMLVT
370 380 390 400 410
AGISPSKRQA REDVQNGAIY INGDRVQDLD YQLSNDDKID DQLTVIRRGK KKYAVLTY