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 Q5KWU5

Entry ID Method Resolution Chain Position Source
AF-Q5KWU5-F1 Predicted AlphaFoldDB

No variants for Q5KWU5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5KWU5

No associated diseases with Q5KWU5

4 regional properties for Q5KWU5

Type Name Position InterPro Accession
domain DHHA1 domain 743 - 883 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 664 - 707 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 9 - 565 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 4 - 720 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
MKKLTSAQVR RMFLEFFQEK GHAVEPSASL IPVDDPSLLW INSGVATLKK YFDGRIVPEN
70 80 90 100 110 120
PRICIVPENP RICNAQKSIR TNDIENVGKT ARHHTFFEML GNFSIGDYFK REAIHWAWEF
130 140 150 160 170 180
LTSDKWIGFD PERLSVTVHP EDEEAYNIWR NEIGLPEERI IRLEGNFWDI GEGPSGPNTE
190 200 210 220 230 240
IFYDRGEAFG NDPNDPELYP GGENDRYLEV WNLVFSQFNH NPDGTYTPLP KKNIDTGMGL
250 260 270 280 290 300
ERMCSILQDV PTNFETDLFL PIIRATEQIA GERYGEDPDK DVAFKVIADH IRAVTFAIGD
310 320 330 340 350 360
GALPSNEGRG YVLRRLLRRA VRYAKHIGID RPFMYELVPV VGEIMHDYYP EVKEKADFIA
370 380 390 400 410 420
RVIRTEEERF HETLHEGLAI LAEVIEKAKE QGSDVIPGEE AFRLYDTYGF PIELTEEYAA
430 440 450 460 470 480
EAGMTVDHAG FEREMERQRE RARAARQDVD SMQVQGGVLG DIKDESRFVG YDELVAASTV
490 500 510 520 530 540
IAIVKDGRLV EEVKAGEEAQ IIVDVTPFYA ESGGQIADQG VFESETGTAV VKDVQKAPNG
550 560 570 580 590 600
QHLHAIIVER GTVKKGSRYT ARVDEAKRMR IVKNHTATHL LHQALKDVLG RHVNQAGSLV
610 620 630 640 650 660
APDRLRFDFT HFGQVKPEEL ERIEAIVNEQ IWKSLPVDIF YKPLEEAKAM GAMALFGEKY
670 680 690 700 710 720
GDIVRVVKVG DYSLELCGGC HVPNTSAIGL FKIVSESGIG AGTRRIEAVT GEAAYRFMSE
730 740 750 760 770 780
QLAILQEAAQ KLKTSPKELN ARLDGLFAEL KELERENESL AARLAHMEAE HLTRQVKDVN
790 800 810 820 830 840
GVPVLAAKVQ ANDMNQLRAM ADDLKQKLGT AVIVLASAQG GKVQLIAAVT DDLVKKGFHA
850 860 870 880
GKLVKEVASR CGGGGGGRPD LAQAGGKDPS KVGEALGYVE TWVKSVS