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 Q6F0Y9

Entry ID Method Resolution Chain Position Source
AF-Q6F0Y9-F1 Predicted AlphaFoldDB

No variants for Q6F0Y9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6F0Y9

No associated diseases with Q6F0Y9

5 regional properties for Q6F0Y9

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 106 - 270 IPR002314
domain Anticodon-binding 289 - 377 IPR004154
domain Aminoacyl-tRNA synthetase, class II 35 - 282 IPR006195
domain Proline-tRNA ligase, class II, C-terminal 406 - 473 IPR016061
domain Prolyl-tRNA synthetase, catalytic domain 13 - 272 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

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
MKQLEKITPR DVDFSQWYTD TVINAKLASY GPVKGTIIFR PYGYAIWELI QKYLDAKFKE
70 80 90 100 110 120
LEVQNVYFPL LIPQSLFQKE KDHIEGFSPE IATVTRVGDT PLPEPLFIRP TSEVLMANFF
130 140 150 160 170 180
KNEVKSYRDL PLIFNQWTNV MRWEKTTRPF LRTSEFLWQE GHTVHSERKE ASDLTLKILD
190 200 210 220 230 240
TYTEFAQNAL LLPVIPGKKT EKEKFAGADS TYTIESLMHD GQALQCGTSH YFADNFSKPY
250 260 270 280 290 300
EIKFQNKEGK LEHAYSTSWG VSTRLIGAII MTHSDDNGLV LPSMVSPVQV RLIQIKETDE
310 320 330 340 350 360
VIKVTEDIKE ALKNKYRVDI DKTDKSFGFK ISEAEIKGIP LRIEIGPRDL ENNQVTISRR
370 380 390 400 410 420
DTREKIQVNV NEVTNIVDQM IKEYDANLYA KALKNREERT SRANSIEEYK NILAQNQGFV
430 440 450 460 470
LVPFCGEIEC EDDVKKQTST NSRCIPFDQD NKTEKCFNCN KDTTLKVYFA RAY