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 A5UMJ1

Entry ID Method Resolution Chain Position Source
AF-A5UMJ1-F1 Predicted AlphaFoldDB

No variants for A5UMJ1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5UMJ1

No associated diseases with A5UMJ1

2 regional properties for A5UMJ1

Type Name Position InterPro Accession
domain Importin-beta, N-terminal domain 31 - 97 IPR001494
domain Exportin-1/Importin-beta-like 103 - 277 IPR013598

Functions

Description
EC Number 6.1.1.3 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.

5 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.
threonine-tRNA ligase activity Catalysis of the reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
threonyl-tRNA aminoacylation The process of coupling threonine to threonyl-tRNA, catalyzed by threonyl-tRNA synthetase. The threonyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a threonine-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
MRILLIHSDY LNYNVKNKTP VAEEIEDAKK QGAFDESLVV FTAVEKDDEN NPQGIVKNLV
70 80 90 100 110 120
KEVIKTNDQV KAENIVLYPY AHLSSSLSSP KVAVQVLKDA EEALDAEGLN VKRVPFGWYK
130 140 150 160 170 180
AFEISCKGHP LSELSRTITA EEEEEEEVEK KPSSWSILDG DKIIDIDDFK FENDQLEKLV
190 200 210 220 230 240
SYELGTGASD AGEPPHVKLM REKELCDYES ASDVGNLKWF PKGRLVRDLL ADYVYNLVVD
250 260 270 280 290 300
QGAMPIETPI FYDLDNEAIN VHAAKFGERQ YRTDTKKNLM LRFACCFGAF RVMADPFITW
310 320 330 340 350 360
KNLPAKLYEL STYSFRFEKK GEVVGLKRLR AFTMPDFHSF CADMNSTLEE FSKQTDMCIQ
370 380 390 400 410 420
TGVDLDVNYE IIFRATKDFY DENKDWMYSI GKKIGKPVLL EILPERKHYW SCKIDFAAID
430 440 450 460 470 480
YLGRPIENPT VQIDVESGKR FDITYLGEDG KEHYPTILHC SPTGSIERVI CSLLEKTAIE
490 500 510 520 530 540
LDEKAPMLPT WLSPIEVRII TVGEDHKDFA NELYDKINAE NIRVDVDDRD ESVGKKIRNA
550 560 570 580 590 600
ATEWIPYIFV VGDNEKESGV FSVTVRETGE KVDMTVDELI KEILDKTKGM PYRGLPLPKD
ISTRINFQ