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 P38708

Entry ID Method Resolution Chain Position Source
AF-P38708-F1 Predicted AlphaFoldDB

2 variants for P38708

Variant ID(s) Position Change Description Diseaes Association Provenance
s08-144386 133 N>S No SGRP
s08-144664 226 A>T No SGRP

No associated diseases with P38708

5 regional properties for P38708

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 283 - 456 IPR002314
domain Anticodon-binding 475 - 575 IPR004154
domain Aminoacyl-tRNA synthetase, class II 225 - 468 IPR006195
domain Proline-tRNA ligase, class II, C-terminal 602 - 688 IPR016061
domain Prolyl-tRNA synthetase, catalytic domain 194 - 458 IPR033721

Functions

Description
EC Number 6.1.1.15 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
aminoacyl-tRNA synthetase multienzyme complex A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates.
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
MPVSEAFAKL CVNEKPPAES AVAVKSLVFK PKTPKSATPV PIVVVALQST TTPSALIANA
70 80 90 100 110 120
TSSKDPRLAR DDLVKQAFQS ESARAFILGD LANATSNFHL LIDHELGTVD GDTILQLNDS
130 140 150 160 170 180
TYMKKSDMMK FLNNFEDSQK VVDFSQEVSK ETATEGKKQQ KKQQPSKAGT AAAAAAAALE
190 200 210 220 230 240
DAKLIGITVD KALDFPGWYQ QILTKGEMLD YYDVSGCYIL RPPSYAIWEN IQKWFDDKIK
250 260 270 280 290 300
AIGVQNAYFP MFVSSRVLEK EKDHVEGFAP EVAWVTRAGS SELEEPIAIR PTSETVMYPY
310 320 330 340 350 360
YAKWVQSYRD LPLKLNQWNS VVRWEFKHPQ PFLRTREFLW QEGHTAHLTA KDAEEEVLQI
370 380 390 400 410 420
LDFYAGVYEE LLAVPVVKGR KTEKEKFAGG DFTTTCEGYI PQTGRGIQGA TSHHLGQNFS
430 440 450 460 470 480
KMFNLSVENP LGSDHPKIFA YQNSWGLSTR VIGVMVMIHS DNKGLVIPPR VSQFQSVVIP
490 500 510 520 530 540
VGITKKTSEE QRKHIHETAR SVESRLKKVG IRAFGDYNDN YTPGWKFSQY ELKGIPIRIE
550 560 570 580 590 600
LGPKDIEKNQ VVVVRRNDSK KYVVSFDELE ARIPEILEEM QGDLFKKAKE LFDTHRVIVN
610 620 630 640 650 660
EWSGFVPALN KKNVILAPWC GVMECEEDIK ESSAKKDDGE EFEEDDKAPS MGAKSLCIPF
670 680
DQPVLNEGQK CIKCERIAVN YCMFGRSY