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 A9W9Q2

Entry ID Method Resolution Chain Position Source
AF-A9W9Q2-F1 Predicted AlphaFoldDB

No variants for A9W9Q2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9W9Q2

No associated diseases with A9W9Q2

5 regional properties for A9W9Q2

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 103 - 271 IPR002314
domain Anticodon-binding 290 - 367 IPR004154
domain Aminoacyl-tRNA synthetase, class II 43 - 283 IPR006195
domain Proline-tRNA ligase, class II, C-terminal 415 - 480 IPR016061
domain Prolyl-tRNA synthetase, catalytic domain 12 - 273 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

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.

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
MPKEVITQRS VDYNQWYLDI VREADLAEVA EVVRGCIVVK AHGWAIWELM QRALDDRIKA
70 80 90 100 110 120
TGHANVQFPL LIPKSFIMKE AEHVEGFAPE VAEVTRAGGE ELAEPYIIRP TSETIIGYFY
130 140 150 160 170 180
SKWIRSYRDL PLLYNQWANV MRWEMRTRPF LRTAEFWWQE GHTAHATEAE AEEETLRILH
190 200 210 220 230 240
DVYADFVEKE MAVPVIRGLK TEKEKFPGAL RSYCIEAMMQ DGRALQAGTS HNLGQNFARA
250 260 270 280 290 300
FDITFTDQNN TIQYAWTTSW GVSTRLIGAL IMTHSDDEGL VLPPRLAPIQ VVVVPIYKND
310 320 330 340 350 360
EERSLVMAAV EQMTAAWKGR LRFKVDDRDN YSPGYKFNEW ELKGVPVRIE VGPKDVAKET
370 380 390 400 410 420
VALARRDIPG KAGKSFVPQA GLTERIEALL NEMQTALFQR ALAFREAHTA DVTSYDELKE
430 440 450 460 470
QIERGFARAY WAGDTADEKR IQEETRATIR CIPLEQPGSV GRCVYTGRET DRQVIFARAY