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 Q5HC27

Entry ID Method Resolution Chain Position Source
AF-Q5HC27-F1 Predicted AlphaFoldDB

No variants for Q5HC27

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5HC27

No associated diseases with Q5HC27

3 regional properties for Q5HC27

Type Name Position InterPro Accession
domain Threonyl/alanyl tRNA synthetase, SAD 671 - 713 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 10 - 573 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 5 - 726 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
MIKHNLVSDL RRLFIDFFVK NGHQFFPSSQ LVIKDDPSLL FTNAGMVQFK QRFTSVDDRS
70 80 90 100 110 120
INTAVSSQKC LRVGGKHNDL ENVGHTNRHH TFFEMLGNFS FGSYFKERAI ELAWDFVTKE
130 140 150 160 170 180
LALDKKRLYI TVYHDDQDAF NLWKKISSFS DDKIIKIKTN DNFWSMGNVG PCGPCSEIFY
190 200 210 220 230 240
DYGESVKGGL PGTPEEDGAR FTEIWNLVFM EYNRTEEGEL SVLPRKCIDT GMGLERIAAV
250 260 270 280 290 300
MQGVHDNYDI NLFKALIAMS KKESGNSSCE IAHRVIADHV RSAAFLIAEG LTPGNEGRDY
310 320 330 340 350 360
ILRRIIRRAA RYVYMLKYTD SLMYKIFPVL IDETSNAYMA DYYPELFKAK DLIISILKTE
370 380 390 400 410 420
EENFKDTLVR ALPLLEKELT YLSTGDVLSG DIIFRLYDTY GFPVDITLDI IKERGIRFDE
430 440 450 460 470 480
KGFYDNMEQQ KTRSRLSHLI KSTEQLNGKI WEDIRQNYNN TRFVGYDNFQ VQSKILSMVM
490 500 510 520 530 540
NNDRNVTVAN VGDKVSILMD ITPFYAEAGG QQADTGLLSV VRRDGKDLFG SSNIADVTNT
550 560 570 580 590 600
KNIFDGLYIH ECIVKSGSLI IGDIVSAEIN SHRRKDLCAN HSATHLLHYI LRMEIDNNIM
610 620 630 640 650 660
QKGSLVGNDK LRFDFSYNMA LTEKQIKLIE NRMCDLIRQN HPVETNICNL QNAMDNGAIA
670 680 690 700 710 720
LFTEKYDNHE VRVVNIGNSK ELCCGTHVKY TGEIGCFKII SESSIACGIR RIEAVTGQYA
730 740 750 760 770 780
IDYFRQQEKV LYQVAESVKS PVEDVLVQID KINRENQELK QKLWAAYFDI IDMQGVNIEK
790 800 810 820 830 840
IGNINFLHGT LSSVPIDVVR KFIMKRLVKD MIMLFSNVVN HNKIYVVGVG NSLHSKVKAA
850 860 870 880
DFVKIIGCVV KSKGGGNAQL AQISTEYIAE VDVIQHIKDE LVSIFNA