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 Q0I8J8

Entry ID Method Resolution Chain Position Source
AF-Q0I8J8-F1 Predicted AlphaFoldDB

No variants for Q0I8J8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0I8J8

No associated diseases with Q0I8J8

6 regional properties for Q0I8J8

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 97 - 481 IPR002314
domain Anticodon-binding 497 - 587 IPR004154
domain Aminoacyl-tRNA synthetase, class II 33 - 490 IPR006195
domain YbaK/aminoacyl-tRNA synthetase-associated domain 259 - 397 IPR007214
domain Prokaryote proline-tRNA ligase core domain 17 - 218 IPR033730
domain Proline--tRNA ligase, anticodon binding domain 495 - 587 IPR044140

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.

3 GO annotations of molecular function

Name Definition
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
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
MRVSRLMLVT LRDVPADAEI ASQQLLIRGG FIRRVGSGIY AYLPLMWRVL QRVMRIVREE
70 80 90 100 110 120
MNQIGALETL LPQLQPAELW EKSGRWQGYT AGEGIMFHLE DRQERSLGLG PTHEEVITEL
130 140 150 160 170 180
ASDLLRSYRQ LPVTLYQIQS KFRDEIRPRF GLMRGREFIM KDAYSFHGDE GDLARMYEEM
190 200 210 220 230 240
EKAYTRVFQR CGLTAVGVDA DSGAIGGAAS QEFMVTADAG EDLILISPDG DYAANQEKAV
250 260 270 280 290 300
SIAPPALPLP SGESRVISTP GQVTIDELCS AQSLHPSQVV KVLLLLAKLE SGDEQPVLVC
310 320 330 340 350 360
LRGDQELNEV KLVNALTQQL DSPVLDLSPI NADQVKTQGL QPLPLGSIGP DLSDHSLAGA
370 380 390 400 410 420
RSWKERFYKL ADTTAAELER FVCGANTSNE HRWGASWSDL GTIPAMDLRN AKAGDHCVHR
430 440 450 460 470 480
PEQSLEERRG IEVGHIFQLG RKYSLSMGAQ ITTKEGKQEH LWMGCYGIGI SRLAQAAVEQ
490 500 510 520 530 540
HHDDAGIIWP LSIAPFQVIV VVANVQDEVQ MALGEEIYNE LLASGIDVLL DDRGERAGVK
550 560 570 580 590
FKDADLIGIP WRVVVGRAAA EGNVELVKRS ERDANVLSRA EAISSLLEAI PTELRIQL