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 Q4AAX3

Entry ID Method Resolution Chain Position Source
AF-Q4AAX3-F1 Predicted AlphaFoldDB

No variants for Q4AAX3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4AAX3

No associated diseases with Q4AAX3

6 regional properties for Q4AAX3

Type Name Position InterPro Accession
domain Peptidase M41 563 - 744 IPR000642
domain AAA+ ATPase domain 341 - 480 IPR003593
domain ATPase, AAA-type, core 346 - 477 IPR003959
conserved_site ATPase, AAA-type, conserved site 448 - 466 IPR003960
domain Peptidase M41, FtsH extracellular 157 - 241 IPR011546
domain AAA ATPase, AAA+ lid domain 509 - 547 IPR041569

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
MSYIEKQEFL TELKTRNILK DISSPEKFFN LKPDQGIYIG FDPTATSLHL GNYISISLLK
70 80 90 100 110 120
RLQKIGIKVL AVIGGATGMI GDPSFSSKER KLLDFKTLNA NKEKIKKQLE SFGLPVFDNF
130 140 150 160 170 180
EIYKNMNILD FLRDVGKNIN ISYLLAKESV ASRIEVGLSF TEFSYQLIQG WDFKFLAENY
190 200 210 220 230 240
QIIGQAGGSD QWGNMVTGLD FIKKSNLVQK DEAFVFTTNL LTDENGQKFG KSLGKPIWLD
250 260 270 280 290 300
PEMYSPFHLY QFLLNQNDEQ AEKIMLWLSF LDLKVINELI FKHKNDKKQR ILQYNLAQEV
310 320 330 340 350 360
VFNIHGDKGL KIAKKITKIL FEKLDYTEIT FKDKLELKKI IPYFKVSFFN ANQIIDLGIF
370 380 390 400 410
KSKRELNEFI SHKALEINGS KISNIGDITE ELKDKSNLFL LRKGKKYFFI IELI