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 B1JDV7

Entry ID Method Resolution Chain Position Source
AF-B1JDV7-F1 Predicted AlphaFoldDB

No variants for B1JDV7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1JDV7

No associated diseases with B1JDV7

4 regional properties for B1JDV7

Type Name Position InterPro Accession
domain Anticodon-binding 351 - 422 IPR004154
domain Aminoacyl-tRNA synthetase, class II 1 - 358 IPR006195
domain Histidyl-anticodon-binding 330 - 422 IPR033656
domain Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain 10 - 318 IPR041715

Functions

Description
EC Number 6.1.1.21 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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
histidine-tRNA ligase activity Catalysis of the reaction: ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His).

1 GO annotations of biological process

Name Definition
histidyl-tRNA aminoacylation The process of coupling histidine to histidyl-tRNA, catalyzed by histidyl-tRNA synthetase. The histidyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3''-OH group of a histidine-accetping tRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSKSLQAIRG MNDILPEQSP LWRYFEGTVA GLLDTYGYSQ IRTPIVEFTE LFKRSIGEVT
70 80 90 100 110 120
DIVEKEMYTF EDRNGDSLTL RPEGTAACVR AVLEHGITGN GQVQKLWYIG QMFRHERPQK
130 140 150 160 170 180
GRYRQFHQIG VEVFNLDGPD IDAELIMLTW RLWGLLGIQD AVKLELNSLG TSEARARYRD
190 200 210 220 230 240
ALVEFLSARL EQLDEDSQRR LKSNPLRILD SKDPNTQAVL VGAPKLEDYL DEDSRVHFEG
250 260 270 280 290 300
LKARLDAAGI PFVINTKLVR GLDYYSKTVF EWVTDKLGAQ GTVCAGGRYD GLVEQMGGKP
310 320 330 340 350 360
TTGVGFAMGI ERLILLLETL GKVPASINRQ IDVYLCAFGE QAELAGLRLS ESLRDRLPGL
370 380 390 400 410 420
RLAVNAGGGS FKSQFKKADK SGALFALILG DDELAKQEIG LKPLRGQGEQ QNIAWDALAE
HLETAIAQA