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 A1KLQ3

Entry ID Method Resolution Chain Position Source
AF-A1KLQ3-F1 Predicted AlphaFoldDB

No variants for A1KLQ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1KLQ3

No associated diseases with A1KLQ3

4 regional properties for A1KLQ3

Type Name Position InterPro Accession
domain DHHA1 domain 754 - 896 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 673 - 717 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 5 - 574 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 1 - 730 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
MQTHEIRKRF LDHFVKAGHT EVPSASVILD DPNLLFVNAG MVQFVPFFLG QRTPPYPTAT
70 80 90 100 110 120
SIQKCIRTPD IDEVGITTRH NTFFQMAGNF SFGDYFKRGA IELAWALLTN SLAAGGYGLD
130 140 150 160 170 180
PERIWTTVYF DDDEAVRLWQ EVAGLPAERI QRRGMADNYW SMGIPGPCGP SSEIYYDRGP
190 200 210 220 230 240
EFGPAGGPIV SEDRYLEVWN LVFMQNERGE GTTKEDYQIL GPLPRNNIDT GMGVERIALV
250 260 270 280 290 300
LQDVHNVYET DLLRPVIDTV ARVAARAYDV GNHEDDVRYR IIADHSRTAA ILIGDGVSPG
310 320 330 340 350 360
NDGRGYVLRR LLRRVIRSAK LLGIDAAIVG DLMATVRNAM GPSYPELVAD FERISRIAVA
370 380 390 400 410 420
EETAFNRTLA SGSRLFEEVA SSTKKSGATV LSGSDAFTLH DTYGFPIELT LEMAAETGLQ
430 440 450 460 470 480
VDEIGFRELM AEQRRRAKAD AAARKHAHAD LSAYRELVDA GATEFTGFDE LRSQARILGI
490 500 510 520 530 540
FVDGKRVPVV AHGVAGGAGE GQRVELVLDR TPLYAESGGQ IADEGTISGT GSSEAARAAV
550 560 570 580 590 600
TDVQKIAKTL WVHRVNVESG EFVEGDTVIA AVDPGWRRGA TQGHSGTHMV HAALRQVLGP
610 620 630 640 650 660
NAVQAGSLNR PGYLRFDFNW QGPLTDDQRT QVEEVTNEAV QADFEVRTFT EQLDKAKAMG
670 680 690 700 710 720
AIALFGESYP DEVRVVEMGG PFSLELCGGT HVSNTAQIGP VTILGESSIG SGVRRVEAYV
730 740 750 760 770 780
GLDSFRHLAK ERALMAGLAS SLKVPSEEVP ARVANLVERL RAAEKELERV RMASARAAAT
790 800 810 820 830 840
NAAAGAQRIG NVRLVAQRMS GGMTAADLRS LIGDIRGKLG SEPAVVALIA EGESQTVPYA
850 860 870 880 890 900
VAANPAAQDL GIRANDLVKQ LAVAVEGRGG GKADLAQGSG KNPTGIDAAL DAVRSEIAVI
ARVG