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 B2J6I0

Entry ID Method Resolution Chain Position Source
AF-B2J6I0-F1 Predicted AlphaFoldDB

No variants for B2J6I0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2J6I0

No associated diseases with B2J6I0

3 regional properties for B2J6I0

Type Name Position InterPro Accession
conserved_site Fumarate lyase, conserved site 281 - 290 IPR020557
domain Fumarate lyase, N-terminal 12 - 306 IPR022761
domain Argininosuccinate lyase, C-terminal 369 - 437 IPR029419

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
MNATQEKLKV QLEQALVAAF GADFAGVDPI LVSASNPKFG DYQANVALSL SKKLGKQPRA
70 80 90 100 110 120
IAGAIVEKLD VSEICEPPEI AGPGFINLKL KTAYLEAQLN DIQADPRLGV PAAKTPKREN
130 140 150 160 170 180
VDFSSPNIAK EMHVGHLRST IIGDSIARIL EFQGHDVLRL NHVGDWGTQF GMLIAYLREV
190 200 210 220 230 240
YPDALTTANA LDIGDLVSFY RKAKQRFDTD TAFQETARQE VVRLQAGAED TLHAWKLLCE
250 260 270 280 290 300
QSRREFQVIY ELLDIKLTER GESFYNPLLS GIVEDLEKSG LLVENQGAKC VFLEGFTNRE
310 320 330 340 350 360
GEPLPLIVQK SDGGYNYATT DLASLRYRIQ QDQAKRIIYV TDAGQGNHFA QFFQVARKAG
370 380 390 400 410 420
WIPDDVELVH VPFGLVLGED GKKFKTRSGD TVRLRDLLDE AVSHAHADLK TRLQKEERQE
430 440 450 460 470 480
TEEFINEVAR VVGISAVKYA DLSQNRTSNY IFSYDKMLDL KGNTAPYMLY VYARIHGISR
490 500 510 520 530 540
KGDINFKELG NNAVLLQHET ELALAKYLLQ LDEVISSVEQ DLLPNRLCEY LFELSQKFNQ
550 560 570 580
FYDRCSILQA EEPQRTSRLV LCDLTARTLK LGLSLLGIQV LERM