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 A5GSC0

Entry ID Method Resolution Chain Position Source
AF-A5GSC0-F1 Predicted AlphaFoldDB

No variants for A5GSC0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5GSC0

No associated diseases with A5GSC0

6 regional properties for A5GSC0

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 97 - 484 IPR002314
domain Anticodon-binding 501 - 589 IPR004154
domain Aminoacyl-tRNA synthetase, class II 33 - 493 IPR006195
domain YbaK/aminoacyl-tRNA synthetase-associated domain 259 - 317 IPR007214
domain Prokaryote proline-tRNA ligase core domain 17 - 218 IPR033730
domain Proline--tRNA ligase, anticodon binding domain 498 - 590 IPR044140

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.

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
MRVSALLLVT LRDDPAEAEI PSHKLLLRGG YIRRVASGIY AYLPLMWRVL RKVSAIVRQE
70 80 90 100 110 120
MDAAGALETL LPQLQPAELW QRSGRWSGYT AGEGIMFHLQ DRQDRELGLG PTHEEVITAL
130 140 150 160 170 180
AADLLRSYRQ LPVNLYQIQT KFRDEIRPRF GLMRGREFIM KDAYSFHASA EDLGRGYAAM
190 200 210 220 230 240
DQAYRRIFSR CGLQVVAVQA DSGAIGGSAS QEFMVTAEAG EDLILSSADG SYAANQERAE
250 260 270 280 290 300
SLPAEPVPLQ SATAAELDTP GQTSIDALVE AQGWHASQLV KVILLVARFE QGRQQPLLVS
310 320 330 340 350 360
LRGDQQLNEV TLANWLNQQH GQAWGALLGI EPLEAKHLAA EKVPAFGYLG PDLSDAVLQG
370 380 390 400 410 420
SKKLESSFLR LADPTALDLP LFICGANRFN AHRLAANWSE PGMASPQRVE LRAALPGDRC
430 440 450 460 470 480
CHDPSQQLQA RRGIEVGHIF QLGLKYSEAL GATFANEQGQ DAPLWMGCYG IGVSRLAQAA
490 500 510 520 530 540
VEQHHDSAGM VWPVPIAPFE VVIVIASSKE AQQVELAEDL YGQLQQAGVD VLLDDRNERA
550 560 570 580 590
GVKFKDAELI GIPWRLVVGR GAVNGQVELV ERCSGEKQEG PHQDLMAQLL QTLDQQRQGL