B4RU34

PR
Gene name
argS
Protein name
Arginine--tRNA ligase
Names
Arginyl-tRNA synthetase, ArgRS
Species
Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype)
KEGG Pathway
amc:MADE_1006385
EC number
6.1.1.19: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

229-298 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B4RU34

Entry ID Method Resolution Chain Position Source
AF-B4RU34-F1 Predicted AlphaFoldDB

No variants for B4RU34

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B4RU34

No associated diseases with B4RU34

2 regional properties for B4RU34

Type Name Position InterPro Accession
domain Arginine repressor, C-terminal 106 - 171 IPR020899
domain Arginine repressor, DNA-binding domain 18 - 82 IPR020900

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
MNIHALLVNR FTEALQEMGV ENAPVPVSRS ARPEFGEYQF NGAMALAKQL KQKPRDIAEK
70 80 90 100 110 120
IVETVKLDDI ASKLEVAGPG FINVHLNDAW LANQCELSLT DPRLGIAKSP EQNIVVDYSS
130 140 150 160 170 180
PNLAKEMHVG HLRTTIIGDA VVKVLEFLGH NVIRQNHMGD WGTQFGMLLA HLSDKLQEEV
190 200 210 220 230 240
AETALSDLED FYREAKVRFD EEEGFADRAR EYVVKLQGGD AQCLALWEKF IDVSITHSEE
250 260 270 280 290 300
VYDKLNVSLT RKDIMGESAY NDDLANVISD LKTKGLAVED QGAQVVFIPE LADKEGNPAV
310 320 330 340 350 360
YIVQKSGGGY LYATTDLAAM RYRSGKLNAD RTLILTDARQ ALHFKQTEIV GRKAGFMKEE
370 380 390 400 410 420
QTYEHCPFGM MLGSDGKPFK TRTGGTVKLV ELLDEAVERA GKLIAERDND LSEEELKEVA
430 440 450 460 470 480
RKVGIGAVKY ADLSKNRTTD YMFNWDSMLS FEGNTAPYLQ YAYTRVKSLF RKAGVDMATM
490 500 510 520 530 540
PVDIKLVEKQ EHALAVLLMQ FEEVIGMVSR EATPHVLCTY LYDVASAFMT FYEACPMLKE
550 560 570
GIEPQVRDSR LALSALVAKT LEKGLTLLGI ETLEKM