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 A6U287

Entry ID Method Resolution Chain Position Source
AF-A6U287-F1 Predicted AlphaFoldDB

No variants for A6U287

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6U287

No associated diseases with A6U287

4 regional properties for A6U287

Type Name Position InterPro Accession
domain DHHA1 domain 735 - 873 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 654 - 697 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 8 - 555 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
MKKLKASEIR QKYLDFFVEK GHMVEPSAPL VPIDDDTLLW INSGVATLKK YFDGRETPKK
70 80 90 100 110 120
PRIVNSQKAI RTNDIENVGF TARHHTFFEM LGNFSIGDYF KQEAIEFAWE FLTSDKWMGM
130 140 150 160 170 180
EPDKLYVTIH PEDMEAYNIW HKDIGLEESR IIRIEGNFWD IGEGPSGPNT EIFYDRGEAY
190 200 210 220 230 240
GQDDPAEEMY PGGENERYLE VWNLVFSEFN HNKDHSYTPL PNKNIDTGMG LERMASVSQN
250 260 270 280 290 300
VRTNYETDLF MPIMNEIEKV SGKQYLVNNE QDVAFKVIAD HIRTIAFAIS DGALPANEGR
310 320 330 340 350 360
GYVLRRLLRR AVRFSQTLGI NEPFMYKLVD IVADIMEPYY PNVKEKADFI KRVIKSEEER
370 380 390 400 410 420
FHETLEDGLA ILNELIKKAK ATTNEINGKD AFKLYDTYGF PIELTEEIAV QAGLKVDMTT
430 440 450 460 470 480
FESEMQQQRD RARQARQNSQ SMQVQSEVLK NITSASTFVG YDTATAQTTL THLIYNGEEV
490 500 510 520 530 540
SQVEAGETVY FMLTETPFYA VSGGQVADTG IVYNDNFEIA VSEVTKAPNG QNLHKGVVQF
550 560 570 580 590 600
GQVNVGATVS AEVNQNDRRD IQKNHSATHL LHAALKSVLG DHVNQAGSLV EADRLRFDFS
610 620 630 640 650 660
HFGPMTNDEI DQVERLVNEE IWKGIDVNIQ EMDIASAKEM GAMALFGEKY GDVVRVVNMA
670 680 690 700 710 720
PFSIELCGGI HVRNTSEIGL FKIVSESGTG AGVRRIEALT GKAAFLYLED IQEKFNTMKS
730 740 750 760 770 780
QMKVKSDDQV VEKLTQLQDE EKALLKQLEQ RDKEITSLKM GNIEDQVEEI NGYKVLVTEV
790 800 810 820 830 840
DVPNAKAIRS TMDDFKSKLQ DTIIILASNV DDKVSMVATV PKSLTNNVKA GDLIKQMAPI
850 860 870
VGGKGGGRPD MAQGGGTQPE NISKSLSFIK DYIKNL