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 B3E044

Entry ID Method Resolution Chain Position Source
AF-B3E044-F1 Predicted AlphaFoldDB

No variants for B3E044

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B3E044

No associated diseases with B3E044

3 regional properties for B3E044

Type Name Position InterPro Accession
domain Threonyl/alanyl tRNA synthetase, SAD 667 - 710 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 6 - 569 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 2 - 723 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
MMNSNEIRQS FLDFFKERGH TILPSASLVP ESPNLLFTNA GMNPFVPFFL GKQKCPYVPP
70 80 90 100 110 120
RIADSQKCLR AGGKHNDLEE VGYDTYHHTF FEMLGNWSFN DYFKEEAIHW AWELLTQKWG
130 140 150 160 170 180
FPKERIYATV YKPAPDEPGE FDEEAFRIWF KLFQKAKLNP LLHIHFGTKK DNFWMMGETG
190 200 210 220 230 240
PCGPCSEIHI DLTPDGQSEG KLINKNSPLC IEIWNLVFIQ LNANEDGSFS LLPSRHVDTG
250 260 270 280 290 300
MGLERVCAII QGTSSFRQFN RTISDYDTDL FIPLIEKLQD ISKVSYTGSI PPTPDFALDP
310 320 330 340 350 360
QLKKDIAFRV IVDHVRALAF AIADGILPSN LGRGHVLRRL LRRAIRFGQI LGVNPPFLFE
370 380 390 400 410 420
MVDPLVKIMG SHYPELIDKQ GHIEEVISSE EELFARTLSH GLALFEEIKQ KMIAEKRKEI
430 440 450 460 470 480
SGKEAFVLYD TYGFPLDLTQ LLAKEQGFSV DTQGFERLMA EQRRRSLLSH EEDIVSLTKT
490 500 510 520 530 540
SQFVGYEELE AEAEVVVLLS ANRAIFDRTP FYAEMGGQVG DKGYVVFDQK KIEVLDTMKS
550 560 570 580 590 600
ASGAHVHRLA FTDDLKPGSR VYLQVDEKRR RCIAAHHTAT HLLHWALRKV LGPETLQRGS
610 620 630 640 650 660
YVGPDRLRFD FSHTGPLSAE ELAEIERLVN EKIELNDPVT AEEESYEKVK NNPDILQLFG
670 680 690 700 710 720
EKYGQRVRIV SVGRYSKELC GGTHVRSTGE IGYFKILGEY GVSAGIRRIE AACGKALEQF
730 740 750 760 770 780
LHAQAAEQDK KWQILHSKDP SLPRLSKWVD TLDLDSLIEI FQRRNEELSS FEKEIKEREK
790 800 810 820 830 840
LRAKKQEENF RREASQQAMA AIAQVEKIGA IPVLFLDCDA KPQSYLPLLW NEISKRIDSV
850 860 870 880 890 900
AILASRSEGK INLFIGVGPS LTTKIEARNL LSQLVASFEG KGGGSKTIAQ GGLKDSIEIS
910 920
SLFEKGRGIL EQYGGQKGQT EPKATG