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 P78600

Entry ID Method Resolution Chain Position Source
AF-P78600-F1 Predicted AlphaFoldDB

No variants for P78600

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P78600

No associated diseases with P78600

4 regional properties for P78600

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 106 - 423 IPR002314
domain Anticodon-binding 463 - 511 IPR004154
domain Aminoacyl-tRNA synthetase, class II 56 - 432 IPR006195
domain Prokaryote proline-tRNA ligase core domain 27 - 421 IPR033730

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
MIIIKRFLHI KTVPKSYGNQ LSKFKYSKQI PTHEVLTKLG YITYPRAGLV NWSKMGLLIQ
70 80 90 100 110 120
NKISQIIRQR MDEIQFEEVS LSLISHKELW KLTNRWDQEE IFKLVGDEYL LVPTAEEEIT
130 140 150 160 170 180
NYVKKQFLES YKNFPLALYQ INPKFRNEKR PRGGLLRGKE FLMKDAYSFD LNESEAMKTY
190 200 210 220 230 240
EKVVGAYHKI FQDLGIPYVK AEADSGDIGG SLSHEWHYLN SSGEDTVFEC NECHNVSNME
250 260 270 280 290 300
KALSYPKEID ETIEVSVIYF TTEDKSTLIC AYYPSNRVLE PKFIQNEIPD IDLDSINDLS
310 320 330 340 350 360
EFNHDISTRI VRIMDSRLSS RSKFPDFPIS NFINRSLITT LTDIPIVLAQ EGEICGHCEE
370 380 390 400 410 420
GKLSASSAIE VGHTFYLGDK YSKPLDLEVD VPTSNNSIEK QRIMMGCYGI GISRIIAAIA
430 440 450 460 470 480
EINRDEKGLK WPRSIAPWEV TVVEVSKQKQ LKNVNDNNHH NNPQDNFQEI YNILNQANID
490 500 510 520 530 540
YRLDNRSDSM GKKLKQSDLL GIPLSIILGN QYPIIEIEVR GNKKNNNNNS WLQSYTENKD
550 560 570
QFDWKVETDA QGNDTKHYIH KDGLVTVVNS LLNDM