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 Q8TWY1

Entry ID Method Resolution Chain Position Source
AF-Q8TWY1-F1 Predicted AlphaFoldDB

No variants for Q8TWY1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8TWY1

No associated diseases with Q8TWY1

1 regional properties for Q8TWY1

Type Name Position InterPro Accession
domain Amidohydrolase-related 50 - 431 IPR006680

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.

5 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).
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
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
MKVDPSEFEL EFFEEIGFER KRCPECGEYF WGPPEAEVCN ETPCVEYSFI GDPPASVKLD
70 80 90 100 110 120
VWEAGEEFFR FFERHDHEVL DRYPVVARWR DDIHLTIASI ACFQPWVTSG EVPPPANPLV
130 140 150 160 170 180
INQPCIRLND IDNVGRTGRH FTLFHMGGHH AFNNHPHDRR DIYWKEETVR LCYEFTVEKL
190 200 210 220 230 240
GIPEEKIAFK ESWWEGGGNA GPCFEVVVDG LELATLVFMQ YEQVGGEYRE LPQKIVDTGY
250 260 270 280 290 300
GIERYAWITT GEPTAYDAVF GDLVDATARD LGVEIDGEAR EILGELARVA GLMDVETESD
310 320 330 340 350 360
LRVLRNRVAR RLDLDVNELV RVAEPVEFVY GILDHARCLA FMLGDGVVPS NAGEGYLARL
370 380 390 400 410 420
VIRRALRLLD GLDAEREYLL EVVERVLEDL RGTYPELAER EEYIQDALEC EIDRYTRALK
430 440 450 460 470 480
RGKKEVRKRL EEKGELSFED LVELYDSHGI PPEVAREIAE DEGVEVEVPD DFYSRVAERH
490 500 510 520 530 540
EGPEEVEEGL EELERIAVEE ELPETELAFY DDEKRLEFKA EVIGTYEVNG DAWVVLDRTY
550 560 570 580 590 600
FYPEGGGQEA DRGTMRWKDG EAEVKDVQKV RGVVFHRIDG DVPPEGAEVE CEVDGERRMR
610 620 630 640 650 660
LTRNHTATHV ILEAARRVLG DHVWQAGAHK STDEARLDVT HHRRISDEEL REIERLANEI
670 680 690 700 710 720
VMKDLPVNKR FMDRNEAERR YGFELYQGGV VPGREIRVVE IEGWNVQACA GTHCDSTGEI
730 740 750 760 770 780
GPIKIVGRER IQDGVERIRF AAGEAALERI WETEDLLRET CEVLRVNPEN LPKTVKRFFE
790 800 810 820 830 840
EWKEQRKRIE RLERELVEAK LRAAPAEGRR VGDFTVTLVE LEDVEVGSVA GTVEELVKEH
850 860 870 880 890 900
ENLVLVAKIV SNGSCQVVVG SGESAPPAGE LMREIGKLIE GGGGGDERLA QGGGRNPDGL
910
TEDRLVEIVE DLAGG