Q9RUW4

PR
Gene name
proS (DR_1266)
Protein name
Proline--tRNA ligase
Names
Prolyl-tRNA synthetase, ProRS
Species
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
KEGG Pathway
dra:DR_1266
EC number
6.1.1.15: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-53 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9RUW4

Entry ID Method Resolution Chain Position Source
AF-Q9RUW4-F1 Predicted AlphaFoldDB

No variants for Q9RUW4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9RUW4

No associated diseases with Q9RUW4

5 regional properties for Q9RUW4

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 116 - 285 IPR002314
domain Anticodon-binding 304 - 396 IPR004154
domain Aminoacyl-tRNA synthetase, class II 50 - 297 IPR006195
domain Proline-tRNA ligase, class II, C-terminal 426 - 499 IPR016061
domain Prolyl-tRNA synthetase, catalytic domain 28 - 287 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
MTKDGGKKDN QGQDKKAQQY GVTPQSVDFN DWYNEVVKKA DLADNSPVAG AMVVRPYGSA
70 80 90 100 110 120
LWENIQRWLD DRFKASGHES LIFPTLIPMN FIMKEADHVE GFAPELFTVN KIGTEELAEP
130 140 150 160 170 180
YVMRPTSETI IGHMWSGWLN SYRDLPFLHY QWGSVFRAEL RTKAFLRTSE FFWHEGHTAH
190 200 210 220 230 240
ADEAEARAEV RQQLDLYHEF CRDVLALPVV RGEKTASERF AGAVATYSIE GMMRDGKALQ
250 260 270 280 290 300
SGTSHYLGQN FSRAFDVKYQ TREQKEEFAH TTSWAISSRI IGAIIMTHGD DSGLMMPPRI
310 320 330 340 350 360
APIQVVVIPV GRKDNFDQMV QEGEKLAAEL RAQGLRVKVD GRDGVTNGFK YNDWELKGVP
370 380 390 400 410 420
VRIELGPRDL ESGVLVVKNR HSEDKETLPR AEAVSGMSAR LDTIHDFLMK RATDFLLANT
430 440 450 460 470 480
AEVDSYDAFQ REIEAGHWVR AYHCGEPACE KSIKEDTKAT ARNVPFDDAE FFAERGEGQC
490
VKCGQPSAYG KRVLFGRQY