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 A8MKD9

Entry ID Method Resolution Chain Position Source
AF-A8MKD9-F1 Predicted AlphaFoldDB

No variants for A8MKD9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8MKD9

No associated diseases with A8MKD9

3 regional properties for A8MKD9

Type Name Position InterPro Accession
domain Arginyl tRNA synthetase N-terminal domain 2 - 87 IPR005148
domain DALR anticodon binding 470 - 587 IPR008909
domain Arginyl-tRNA synthetase, catalytic core domain 109 - 455 IPR035684

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
MELLIKQISA FVEDVFEQKG YDKKYGMVTV SDRPDLCQFQ CNGALPAAKE YKKAPIQIAN
70 80 90 100 110 120
DLLPALKNVE IFEEITIAGP GFININVKDS FLAAYVNEMY GSEKLGLEEP AEPQTIIIDY
130 140 150 160 170 180
GGANVAKPLH VGHLRAAIIG ESLKRISRFV GHKVIGDVHL GDWGLQMGMV ISELRRRSPH
190 200 210 220 230 240
LPYFDESYEG EYPAEAPFTI DELEDIYPAA SKLAKSDAAA MEEAQQATAE LQKGRRGYMA
250 260 270 280 290 300
LWQHILNVSV ADLKKGYGNL NVDFDLWNGE SDCQKYIDVM VDYLKKNNYT SFSDGLLIVD
310 320 330 340 350 360
VAKETDNHVI PPFIVLKTDG SSLYSTTDLA TIWERVQDYD PDQIIYVVDK RQELHFEQVF
370 380 390 400 410 420
RCAKKTKIAG EDLTLKFLGF GTMNGKDGKP FKTREGGVMR LQDLIQIIKD AVYNKLQENE
430 440 450 460 470 480
AIDPSEVDEI SRKVGLAALK YGDLSNQITK DYVFDIDRFA SFEGNTGPYI LYTIVRIKSI
490 500 510 520 530 540
LRRIAAEGFQ ASDKIGVPHS DVERSLLLKL SRFNETVEFS FVNHSPNRIC DYIYDLANTF
550 560 570 580
NKFYHDTKII SETEFEKKSS WINLITLTMN VLETCLELLG IEAPEKM