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 Q49Y56

Entry ID Method Resolution Chain Position Source
AF-Q49Y56-F1 Predicted AlphaFoldDB

No variants for Q49Y56

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q49Y56

No associated diseases with Q49Y56

4 regional properties for Q49Y56

Type Name Position InterPro Accession
domain DHHA1 domain 736 - 873 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 654 - 697 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 8 - 556 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 4 - 710 IPR018165

Functions

Description
EC Number 6.1.1.7 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.

4 GO annotations of molecular function

Name Definition
alanine-tRNA ligase activity Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
alanyl-tRNA aminoacylation The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine 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
MKNLKASEIR QNFIDYFVEK GHMVEPSAPL VPIDDDSLLW INSGVATLKK YFDGRETPRK
70 80 90 100 110 120
PRIVNSQKAI RTNDIENVGF TARHHTFFEM LGNFSIGDYF KQEAIEFAWE FLTSEKWMAM
130 140 150 160 170 180
EPKLLYVTIH PEDKEAYRIW NEDIGLEESR IIRIEGNFWD IGEGPSGPNT EIFYDRGEDF
190 200 210 220 230 240
GQDDPAEEMY PGGENERFLE VWNLVFSEFN HNKDHTYTPL PNKNIDTGMG LERMASLAQN
250 260 270 280 290 300
VRTNYETDLF MPIIHEVEKV SGKTYLENDN YDVAFKVIAD HIRTIAFAIA DGALPANEGR
310 320 330 340 350 360
GYVLRRLLRR AVRFSQSLDI NEPFMYRLVD IVADIMEPYY PNVKEKADFI KRVIKSEEER
370 380 390 400 410 420
FHETLEEGLA ILNNLVAQAK TSTHEISGKD AFKLYDTYGF PVELTEEIAT QENLSIDMQT
430 440 450 460 470 480
FEEEMQQQRD RARQARQNSQ SMQVQSEVLK KITTDSTFVG YDVMDKASVI TDIIQNGELV
490 500 510 520 530 540
ESAEAGETIY FILRETPFYA VSGGQVADQG TISNENFEIA VTEVTKAPNG QNLHKGEIQF
550 560 570 580 590 600
GTVKKNAEVS ASVNHKERRS IKKNHSATHL LHAALKEVLG DHVNQAGSLV EADRLRFDFS
610 620 630 640 650 660
HFGPMTQEEI DTVERRVNEE IWNSIEVDIQ EMPISEAKQL GAMALFGEKY GEIVRVVNMA
670 680 690 700 710 720
PFSIELCGGI HVNNTAEIGL FKIVSESGTG AGVRRIEALT GKSAFLYLET IQSQFNAVKS
730 740 750 760 770 780
QVKVKSDDQV LEKIVHMQDE EKELTKQLEQ KNKEVTSLKM GDITNQVEEI NGLKVLATEV
790 800 810 820 830 840
DVPNAKAIRE TMDDFKSKLQ DTVIVLISNI DGKVSLVATV PKALTDKVKA GDIIKNMAPV
850 860 870
VGGKGGGRPD MAQGGGTEPK NITESLRFIK DYIKSL