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 P57933

Entry ID Method Resolution Chain Position Source
AF-P57933-F1 Predicted AlphaFoldDB

No variants for P57933

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P57933

No associated diseases with P57933

4 regional properties for P57933

Type Name Position InterPro Accession
domain DHHA1 domain 732 - 870 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 652 - 695 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 6 - 554 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 2 - 708 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
MKTTAEIRQS FLDFFHTKGH QIVASSALVP ENDPTLLFTN AGMNQFKDVF LGMDKRPYSR
70 80 90 100 110 120
ATTAQRCVRA GGKHNDLENV GYTARHHTFF EMLGNFSFGD YFKKDAIHFG WEYLTSPRWL
130 140 150 160 170 180
GLPAEKLWVT VYETDDEAYD IWNKEVGVPA ERIIRIGDNK GAPYASDNFW AMGDTGPCGP
190 200 210 220 230 240
CTEIFYDHGE HIWGGPPGSP EEDGDRYIEI WNIVFMQFNR HADGTMEPLP KPSVDTGMGL
250 260 270 280 290 300
ERISAVLQHV NSNYEIDIFQ KLIAKVAELT GEKDLSNKSL RVIADHIRSC AYLIADGVIP
310 320 330 340 350 360
SNEGRGYVLR RIIRRAVRHG NLLGAKEAFF YKLVPTLIDV MAEAGIGVKE KQATVEKLLR
370 380 390 400 410 420
LEEEQFARTL ERGLALLDEA LANVKKGELS GEVAFKLYDT YGFPLDLTAD VCRERNITID
430 440 450 460 470 480
EVGFDREMEA QRLRAQSASQ FGMDYNNVIR VEGCTTFEGY TASESLAKVT ALFADGKPVE
490 500 510 520 530 540
RIEAGQSAVV ILENTPFYAE SGGQIGDSGY LNGQGFSFEV KDTQKYGQVF GHIGELVSGS
550 560 570 580 590 600
LTVGKSVNAV VDVKRRHNTS LNHSATHLLH AALRQVLGEH VVQKGSLVSD VALRFDFAHH
610 620 630 640 650 660
EAITKAQLVE IECLVNQQIR ANHLIQTELM ELEAAKAKGA MALFGEKYAD QVRVLTMGDF
670 680 690 700 710 720
SIELCGGIHA KRTGDIGLCK ITTETAIAAG IRRIEAITGE NAMSWLHQQQ ALLAQSADLL
730 740 750 760 770 780
KSDVNSIVEK IQQLQDKAKK AEKELQVLKE KSAMQAGSDL ARSAVKINDV SVIVQKLDGV
790 800 810 820 830 840
DTKSLRVVVD DLKNQLSSAV IVFASVVEEK VNLIVGVTSD LTSKVKAGEL VNLLAQQVGG
850 860 870
KGGGRPDMAM AGGTQIENVD HALSFATTWL KENL