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 Q14HB9

Entry ID Method Resolution Chain Position Source
AF-Q14HB9-F1 Predicted AlphaFoldDB

No variants for Q14HB9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q14HB9

No associated diseases with Q14HB9

4 regional properties for Q14HB9

Type Name Position InterPro Accession
domain DHHA1 domain 723 - 859 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 643 - 686 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 6 - 544 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 2 - 699 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
MITTKELRNK FINYFESKNH SHQPSSSLIP FGDDTLLFTN AGMVQFKDVF LGIEKKDFSR
70 80 90 100 110 120
AVTVQKCLRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKKEAISFA WEFLTKEIKL
130 140 150 160 170 180
PVEKLWVTIY ASDDEAFDVW HKHIGLAKER IIRIDSSDNF WSMGDTGPCG PCTEIFYDHG
190 200 210 220 230 240
EDVAGGLPGT PEQDGDRYIE IWNIVFMQYN RHADGSTTDL PKPSVDTGMG LERISAVLQN
250 260 270 280 290 300
VHSNYEIDLF QALIKKAQQV THAKDINSPS LKVIADHIRA CAFLIADGVL PANEGRGYVL
310 320 330 340 350 360
RRIIRRAIRH GNKVGAKEIF FYKLVAELVS QMGEVYSQLI DKRELIEKTL IKEEELFLKT
370 380 390 400 410 420
IENGIKIFDA EIENLKDNTI SGEVAFKLYD TYGFPFDLTA DMAREKGLKV DEQAFLAQMQ
430 440 450 460 470 480
IQKQRSKEAG KFNVDYNSLI NSQVKSEFRG YSTLIEDAKV LEIYQDGQLV ASTSEQVSAV
490 500 510 520 530 540
VVLDKTPFYA ESGGQVGDKG ILEGIGFEFV VEDVQKSGEA ILHIGKLVKG HLNLNDELTA
550 560 570 580 590 600
RVSDKPRLAT AANHSATHLL HKALKLVLGG HAEQKGSLVD ENRLRFDFTH DKAISRSKIE
610 620 630 640 650 660
QIELLVNQQI RANYPVTTIE TSQQKAKSLG AEALFGEKYG DIVRVISMGD FSIELCGGTH
670 680 690 700 710 720
VAYTGDIGLF KVTSEGSIAS GVRRIEAVTA DKAIRHTFTN ENKIIAIKDS LKANDTNLID
730 740 750 760 770 780
KIKSMLEQIK NQEKQIAKLK KELLSGSSND IKETNIGDIK VVVANVDGVD VKTLRNKIDD
790 800 810 820 830 840
YKSKNTKVIA VLTTTNADKV QFVIGVSNAL TTLIKAGDIA KELSSHIDGK GGGRADMAQG
850 860
GGNNSANIDQ ALSQVEKFIL NNIKE