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 A2BR45

Entry ID Method Resolution Chain Position Source
AF-A2BR45-F1 Predicted AlphaFoldDB

No variants for A2BR45

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2BR45

No associated diseases with A2BR45

6 regional properties for A2BR45

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 53 - 64 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 23 - 183 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 427 - 601 IPR002300-2
domain Aminoacyl-tRNA synthetase, class Ia 622 - 661 IPR002300-3
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 699 - 818 IPR013155
domain Leucyl-tRNA synthetase, editing domain 234 - 411 IPR025709

Functions

Description
EC Number 6.1.1.4 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.

3 GO annotations of molecular function

Name Definition
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
leucine-tRNA ligase activity Catalysis of the reaction: L-leucine + ATP + tRNA(Leu) = AMP + diphosphate + 2 H(+) + Leu-tRNA(Leu).

1 GO annotations of biological process

Name Definition
leucyl-tRNA aminoacylation The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MISPDKRYEA DTNLYNPSEI EKKWQSIWTE NNLYKTDELT ENSDKFYALS MFPYPSGNLH
70 80 90 100 110 120
MGHVRNYVIT DLIARFQRFK GKSVLHPMGW DAFGLPAENA AIERGISPSV WTKKNISHMK
130 140 150 160 170 180
SQLKLLGLSV DWDREFATCD ENYYIWTQYL FLELYKSGLV YQKESEVNWD PIDNTVLANE
190 200 210 220 230 240
QVDSEGKSWR SGAVVEKKLL KQWFLRITNY ADELLKDLEK LDNWPERVKI MQDNWIGKSI
250 260 270 280 290 300
GANINFNINT NPEKNITVFT TRPDTLFGVT YLAISVNHSL IKKITDQETI QDIENLKQYL
310 320 330 340 350 360
KDNKNNELEK IGIKTSLIAI NPVNSEPIPI WVASYVLDEY GTGAVMGVPA HDLRDFEFAK
370 380 390 400 410 420
KNNIDIKQVI VKDKSEQSNE LDNAYVENGY LINSNHYNGL ANTIAKLKIA EEGVNNGWAE
430 440 450 460 470 480
NKIQYRLRDW LISRQRYWGC PIPIVNCKKC GAVPLNQSDL PVSLPKDIEI SANKINALGN
490 500 510 520 530 540
NNDWINTTCP KCGIGARKET DTMDTFMCSS WYFLRYPSSK CSTKPFEKNE INKWLPVDQY
550 560 570 580 590 600
VGGVEHAILH LLYARFFTKA LRDNELFDID EPFKKLLTQG MVQSAAYKNN KTGKYVSPSD
610 620 630 640 650 660
ITDLSNPTDP IDNSKLEVLF EKMSKSKYNG IDPESVIKKY GADTARMFIL FKAPPEKDLE
670 680 690 700 710 720
WGDTDVEGQF RFLSRIWKLY INCAKNINSK SNSHPDKEKS LIKSMNIAIK EISNDILNNQ
730 740 750 760 770 780
FNTAISELMK FYNSLSNSIN DINNNLKIDA LKTFCILLAP FAPHIAEEIW HLIGFKKSVH
790 800 810 820 830 840
LEHWPSFNAE ALKEDSYELV IQVNGKVRDK VNINNDMSED QIKELTLKRP NILKWTQDKE
850
IRKIIIVKGK IMNIVV