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 Q9XDM3

Entry ID Method Resolution Chain Position Source
AF-Q9XDM3-F1 Predicted AlphaFoldDB

No variants for Q9XDM3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9XDM3

No associated diseases with Q9XDM3

4 regional properties for Q9XDM3

Type Name Position InterPro Accession
domain DHHA1 domain 727 - 865 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 648 - 691 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 7 - 551 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 3 - 704 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
MGFSAHEIRE LFLSFFEKKG HTRVKSAPLV PENDPTLLFV NAGMVPFKNV FLGLEKRPYK
70 80 90 100 110 120
RATSCQKCLR VSGKHNDLEQ VGYTSRHHTF FEMLGNFSFG DYFKKEAIEY AWEFVTEVLK
130 140 150 160 170 180
LPKERLYVSV YKDDEEAYRI WNEHIGIPSE RIWRLGEEDN FWQMGDTGPC GPSSEIYVDR
190 200 210 220 230 240
GEEYEGEERY LEIWNLVFMQ YNRDENGVLT PLPHPNIDTG MGLERIASVL QGKNSNFEID
250 260 270 280 290 300
IIYPLIEFGE EVSGKKYGEK FETDVALRVI ADHLRAITFA ISDGVIPSNE GRGYVIRRIL
310 320 330 340 350 360
RRAMRFGYQL GITEPFLYKG IDLVVDIMKE PYPELELSRD FVKGIVKGEE ERFIRTLRSG
370 380 390 400 410 420
MEYIQEVIEK ALSEGRKTLT GKEVFTAYDT YGFPVDLIQE IAKEKGLEID LEGFQCELEE
430 440 450 460 470 480
QRERARKSFK IETKEVKPVY AHLKELGITS RFVGYEHLEY ETEVLGIIVG DEIVSEIKEG
490 500 510 520 530 540
EEGEIILRET PFYPEGGGQI GDSGIIETDK GIFKVEDTQR PTEGIIVHIG KLLKGKISVK
550 560 570 580 590 600
DIVHARVDKE RRWDIMRNHT ATHLLHAALR NLLGEHVRQA GSLVADKYLR FDFTHFSPLT
610 620 630 640 650 660
EEEIKRIEEL VNEKIRENLP VSVMEMAYQE ALQTGAIAIF EEKYGERVRV ISCGEFSKEL
670 680 690 700 710 720
CGGTHVSATG DIGYFKIISE SSVGAGVRRI VAQTGRWAVN TAFEEHTTLK KVSNALGVKE
730 740 750 760 770 780
DEVVQKVEEL KEEIKEKEKE IQKLRQEILK LQIREKVKEE RHRELTLYYG VFEDVEPEEL
790 800 810 820 830 840
RNLADILRQR TGKDVVFIAS KKEGKINFVI ASSKGISKEV RANELIRQVG KVLKGGGGGR
850 860 870
EDLAQGGGKA PDKFDESVKL LKELLSGVSV G