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 Q8Y193

Entry ID Method Resolution Chain Position Source
AF-Q8Y193-F1 Predicted AlphaFoldDB

No variants for Q8Y193

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8Y193

No associated diseases with Q8Y193

4 regional properties for Q8Y193

Type Name Position InterPro Accession
domain DHHA1 domain 743 - 880 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 663 - 705 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 5 - 564 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 1 - 718 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
MKASDIRQKF LTFFETKGHT VVRSSPLVPG NDPTLLFTNS GMVQFKDVFL GTDKRPYVRA
70 80 90 100 110 120
ASVQRCLRAG GKHNDLENVG YTARHHTFFE MLGNWSFGDY FKRDALVWAW ELLTQEYKLP
130 140 150 160 170 180
ADKLWATVYQ TDDEAYDIWT KVIGLPPERV VRIGDNKGAP YASDNFWQMA ETGPCGPCSE
190 200 210 220 230 240
IFYDHGPEIW GGPPGSPEAD GDRYIEIWNN VFMQFDRQLD PQTGEYTLTP LPAPCVDTGM
250 260 270 280 290 300
GMERLAAILQ HVHSNYEIDL FQALVSAAAR ETNTKDLANN SLRVIADHIR ACAFLIVDGV
310 320 330 340 350 360
IPGNEGRGYV LRRIIRRAIR HGYKLGCRAA FFHKLVDDLV KEMGEAYPEL REARDRVVDV
370 380 390 400 410 420
LRTEEARFFE TIEHGMSILD GALGELKAAG KDEKQRMLDG ELAFKLHDTY GFPLDLTQDV
430 440 450 460 470 480
CRENDVIVDE AAFDAAMNRQ REQARAAGKF KMAAGTLDYT GDKTTFHGYD QLLSETSRVT
490 500 510 520 530 540
ALFVDGASVP EMRPGQTGVV VLDHTPFYAE SGGQVGDQGT LKAATVWFDV ADTQKVLPEV
550 560 570 580 590 600
FGHQGTLRTG VLKVGDAVGA EVDAVRRART MRNHSATHLM HKALREVLGA HVQQKGSLVD
610 620 630 640 650 660
ADKTRFDFSH NTPMTPLQIR EVEARVNAEI LANASTNAQM MGFDDAVKSG AMALFGEKYG
670 680 690 700 710 720
DEVRVLTIGS SKELCGGTHV ARTGDIGLFK IVGESGVAAG IRRVEAITGD NVLHYLQTLD
730 740 750 760 770 780
TRIGEAAAAL RAQPSELTQR IVQVQDQVKS LEKELERLKS KLAASQGDEL VSQAVDVAGI
790 800 810 820 830 840
KVLAAKLDGA DAKTLRETMD KLKDKLKTAA IVLGSVSDGK VALIAGVTAD ATARIKAGEL
850 860 870 880
VNFVAQQVGG KGGGRPDMAQ AGGTEPDKLP QALAGVTAWV QQKV