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 Q18JG3

Entry ID Method Resolution Chain Position Source
AF-Q18JG3-F1 Predicted AlphaFoldDB

No variants for Q18JG3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q18JG3

No associated diseases with Q18JG3

5 regional properties for Q18JG3

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 106 - 276 IPR002314
domain Anticodon-binding 295 - 390 IPR004154
domain Aminoacyl-tRNA synthetase, class II 19 - 288 IPR006195
domain Proline-tRNA ligase, class II, C-terminal 417 - 512 IPR016061
domain Prolyl-tRNA synthetase, catalytic domain 19 - 278 IPR033721

Functions

Description
EC Number 6.1.1.15 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.
proline-tRNA ligase activity Catalysis of the reaction: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

1 GO annotations of biological process

Name Definition
prolyl-tRNA aminoacylation The process of coupling proline to prolyl-tRNA, catalyzed by prolyl-tRNA synthetase. The prolyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a methionine-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
MSEDQDLGIT QSKIHNTGEW YAEVVQKAEL ANYGPEGMSG FIVTRPRAYG LWERVQSYLD
70 80 90 100 110 120
TRFKQTGVQN AYFPLFIPEG YLEREKEIVE GFDPEVAWVE QAGRNELEER LAVRPTSESI
130 140 150 160 170 180
IAPYLSQWIR SYRDLPLRVN QWTSVVRWEA TETKPFFRTK EFLWQEGHTA HATRADAWAE
190 200 210 220 230 240
TMLRLNQYES TYEDLLAIPV LQGAKPEHDK FPGADTTTTV EALMPDGKSV QGATSHYLGT
250 260 270 280 290 300
EFADAFDITY TDTDETSRVA HTTSWGLSWR ALGALIMTHS DNQGLVLPPT VAPEQVVIVP
310 320 330 340 350 360
IWQTETKERV LEYAEDVANN LDDAGIRVEL DDRDDQNPGF KFNEWELKGV PLRAEIGPDE
370 380 390 400 410 420
ATEGTVTLIH RPDGESITAE RSEIVETVQE QFDAVYAKLY AAAEETLNSN IRIAETRSEL
430 440 450 460 470 480
LGTIGQHGGY VKTPWCGDEG CETAIKDEIA AEIVMVPISS DEDDEQDTTD ENMGVNNDTT
490 500 510
VESNEKSLDL TDSTCVVCDN PAFKTAYFAK SY