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 Q7MV54

Entry ID Method Resolution Chain Position Source
AF-Q7MV54-F1 Predicted AlphaFoldDB

No variants for Q7MV54

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7MV54

No associated diseases with Q7MV54

4 regional properties for Q7MV54

Type Name Position InterPro Accession
domain DHHA1 domain 732 - 868 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 654 - 696 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 6 - 543 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 2 - 709 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
MLTSKEIRES FKTFFASKGH KIVPSAPMVI KGDPTLMFTN AGMNQFKDII LGNTEAKYTR
70 80 90 100 110 120
VADSQKCLRV SGKHNDLEEV GHDTYHHTMF EMLGNWSFGD YFKKEAIEWA WEYLVTVLGL
130 140 150 160 170 180
DPQRLYATVF EGNPEEGLDR DNEAASYWAQ FLPEERIING NKHDNFWEMG DTGPCGPCSE
190 200 210 220 230 240
IHIDLRSDEE RAQINGLELI NKSHPQVIEI WNLVFMQYNR KADASLTPLP HKVIDTGMGF
250 260 270 280 290 300
ERLCMALQGK TSNYDTDVFQ PLIRTLATMT GIGYGEDSTS DIAMRVVADH IRTIAFAITD
310 320 330 340 350 360
GQLPSNAKAG YVIRRILRRA VRYGYTFLHC REAFMYRLLP TLIDTMGDAY PELQAQRELI
370 380 390 400 410 420
SRVIKEEEES FLRTLETGIR LLEKKIADNK ATGSTVLDGV AAFELYDTFG FPLDLTALIL
430 440 450 460 470 480
SENGMTVDES GFDTEMQKQK ERARNAAAVE AGDWVVLREG ESKFSGYDFT ETETEILRYR
490 500 510 520 530 540
QVKQKNKEYF QVVLSDTPFY AEMGGQVGDS GQLIDESGVA YDIFDTKREN NLSVHLMKKL
550 560 570 580 590 600
PESTTDTFVA RINQDKRRQA EANHTATHLL HEALREVLGT HVEQKGSFVS PEVLRFDFSH
610 620 630 640 650 660
FGKMSPEEIR KVEELVSERI RADFQREEFR DVPIAEAQAM GAMALFGEKY GEEVRVLKYG
670 680 690 700 710 720
SSVELCGGTH IPSTGMIGAF RIVTESSIAS GVRRIEAVTG IGAERFIYEK EDILLAVKEL
730 740 750 760 770 780
FNNNPNLIKS IKKMLEEDAS LKKQIADMKH ERMLKFKKSL LEQDVRRRGI RLFLFQEIME
790 800 810 820 830 840
AETAKDIAFQ IAGELQESFV LIAGTTEGGE KCALTVMLSK DLTEGGMDAA KLVRSAAKHI
850 860 870
QGGGGGQPHF ATAGGKNPKG LPAAIQQILT EAELTD