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 C1CAS7

Entry ID Method Resolution Chain Position Source
AF-C1CAS7-F1 Predicted AlphaFoldDB

No variants for C1CAS7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C1CAS7

No associated diseases with C1CAS7

2 regional properties for C1CAS7

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 39 - 49 IPR001412
domain RNA-binding S4 domain 353 - 414 IPR002942

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
MHIFDELKDR GLIFQTTDEE ALRKALEEGQ VSYYTGYDPT ADSLHLGHLV AILTSRRLQL
70 80 90 100 110 120
AGHKPYALVG GATGLIGDPS FKDAERSLQT KDTVDGWVKS IQGQLSRFLD FENGENKAVM
130 140 150 160 170 180
VNNYDWFGSI SFIDFLRDIG KYFTVNYMMS KESVKKRIET GISYTEFAYQ IMQGYDFFVL
190 200 210 220 230 240
NQDHNVTLQI GGSDQWGNMT AGTELLRRKA DKTGHVITVP LITDATGKKF GKSEGNAVWL
250 260 270 280 290 300
NPEKTSPYEM YQFWMNVMDA DAVRFLKIFT FLSLDEIEDI RKQFEAAPHE RLAQKVLARE
310 320 330 340 350 360
VVTLVHGEEA YKEALNITEQ LFAGNIKNLS VKELKQGLRG VPNYQVQADE HNNIVELLVS
370 380 390 400 410
SGIVNSKRQA REDVQNGAIY VNGDRIQDLD YVLSDADKLE NELTVIRRGK KKYFVLTY