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 C5ZZZ3

Entry ID Method Resolution Chain Position Source
AF-C5ZZZ3-F1 Predicted AlphaFoldDB

No variants for C5ZZZ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C5ZZZ3

No associated diseases with C5ZZZ3

5 regional properties for C5ZZZ3

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 136 - 145 IPR001412
domain Arginyl tRNA synthetase N-terminal domain 12 - 96 IPR005148
domain DALR anticodon binding 522 - 644 IPR008909
domain Arginyl-tRNA synthetase, catalytic core domain 106 - 367 IPR035684-1
domain Arginyl-tRNA synthetase, catalytic core domain 390 - 496 IPR035684-2

Functions

Description
EC Number 6.1.1.19 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.

2 GO annotations of molecular function

Name Definition
arginine-tRNA ligase activity Catalysis of the reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

1 GO annotations of biological process

Name Definition
arginyl-tRNA aminoacylation The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. The arginyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of an alanine 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
MTYDDIKAKV GELLKTIISE MLEKEGKTWE GEILFDETPN MEFGDFATTV AFLLAKVFKK
70 80 90 100 110 120
APRIIAQEIA SNLEDKLPEY IAKVEVAGAG YINFFLDYEK FSKLTVKEIL QKGEHFGESK
130 140 150 160 170 180
IGEGKKVIVE HTSVNPTKPL HMGHARNAVL GDTVARIMRA LGYNVEVQNY IDDLGVQFAQ
190 200 210 220 230 240
VLWGYLNMRE EFESIIKELK EKGLSKEDIL DHALGLLYVE VHKKMEEYPE VEREIRSIMK
250 260 270 280 290 300
ELEKEDNEIS EKGRKLAEDV VKAQMKTTYR LSISYDLLSW ESDIVRSGIF EESYKRIQEN
310 320 330 340 350 360
SHFEWAQEGK YKGAFIMKLG DLFPDLENPD TVLIRSDGTA TYTGKDIAYH LWKFGKVSAD
370 380 390 400 410 420
MRYKVWDKIN DHKTWTTAKD GERMPGRFAN AEIVINVVGS EQRYEQMAVA YALKLLGYEE
430 440 450 460 470 480
EYHNFHHLAY EHVVRPEGKF SGRKGTWIGF TVDEVLDEAV KRAKELVEEK NPSLSGEEKE
490 500 510 520 530 540
KIAEIVGVGA VRYNLVKYSP EKIITFRWED VLNFEGESAP YIQYAHARCA SILKKAMEEG
550 560 570 580 590 600
INIDKDALLK NADFSKLDNK EKELIKIISK FPEIVKTAGR DIKPHLLATY ANELAMVFNS
610 620 630 640
FYMALPVLKA EEGVRELRLL LVIATKQVLK NTLGLMGIEA PEVM