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 Q0AZQ1

Entry ID Method Resolution Chain Position Source
AF-Q0AZQ1-F1 Predicted AlphaFoldDB

No variants for Q0AZQ1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0AZQ1

No associated diseases with Q0AZQ1

4 regional properties for Q0AZQ1

Type Name Position InterPro Accession
domain DHHA1 domain 736 - 875 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 656 - 699 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 6 - 557 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 2 - 712 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
MWSSAEIRKT FLEYFEERGH SVVESSSLVP VNDPTLLFTN AGMNQFKDVF LGLDKRKYVR
70 80 90 100 110 120
ATSSQKCVRA GGKHNDLDTV GRTPRHHTFF EMLGNFSFGD YFKREAIGYA WEFLTEVVGL
130 140 150 160 170 180
PEEKLWVTIY QDDDEAADLW PEISGIDPGR IVRLGEKDNF WSMGDTGPCG PCSEILYDRG
190 200 210 220 230 240
IEYSCGAPDC GIGVCDCDRW LEIWNLVFMQ FNRDESGEMT PLPRPSIDTG MGLERLSSIL
250 260 270 280 290 300
QGVDSNFDTD LFIPIIKRIE ELTGKAYEQG ERGFPFRVIA DHSRACSFLI ADGVLPSNDG
310 320 330 340 350 360
RGYVLRRILR RALRFGRFLG IEGSFLYKNV DVVCDIMQEA YPELLEKQDF IKEVIRLEEE
370 380 390 400 410 420
RFLLTLNDGL KKAEEIMERA RQRGDNVIPG EEAFMLYDTY GFPLDLTEDM AEENQFTLDK
430 440 450 460 470 480
AGFDRSMEEQ RQRARQANKG EDLLGQERLL SEKLAGIAPS SFTGYENSRD ESVLLAIIKG
490 500 510 520 530 540
SELMDKALNG EEVILITART PFYAESGGQV ADCGIIKGQE GLLRVQDVKK LSAWILHYGI
550 560 570 580 590 600
VEGVLTTGEG VSLQLDDPAR MDTARNHTAT HLLHRALREV LGEHAQQKGS LVEPARLRFD
610 620 630 640 650 660
FSHLKALSSE ELSRIEQMVN EAIWKLYPVT TTVTALGQAR EMGAMALFGE KYGEEVRVVQ
670 680 690 700 710 720
VDTYSSELCG GTHVQNTGQI GLFKITGEGS IGSGLRRIEA ITGSYALEYI KQLEDELKKA
730 740 750 760 770 780
ASALRSSPLE LAKRIENLNN SLKEKDKEIE NLLQRLSRSS SDELVNKAFQ LNDAWILIEE
790 800 810 820 830 840
VDIEDPGSLR QNAEMLKDKL GRAIVMLASI KGEKVSFVCF VSKDLLEQGL HAGKIVAAAA
850 860 870
QVAGGGGGGR PDMAQAGGRD KSKISEALAE ARKMVKKTLS