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 A2RIS0

Entry ID Method Resolution Chain Position Source
AF-A2RIS0-F1 Predicted AlphaFoldDB

No variants for A2RIS0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2RIS0

No associated diseases with A2RIS0

4 regional properties for A2RIS0

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 11 - 22 IPR001412
domain Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain 5 - 323 IPR020058
domain Glutamyl-tRNA synthetase 5 - 331 IPR033910
domain Aminoacyl-tRNA synthetase, class I, anticodon-binding 344 - 482 IPR045462

Functions

Description
EC Number 2.1.2.1 Hydroxymethyl-, formyl- and related transferases
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.

2 GO annotations of molecular function

Name Definition
glycine hydroxymethyltransferase activity Catalysis of the reaction: 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.
pyridoxal phosphate binding Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.

2 GO annotations of biological process

Name Definition
glycine biosynthetic process from serine The chemical reactions and pathways resulting in the formation of glycine from other compounds, including serine.
tetrahydrofolate interconversion The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesise other tetrahydrofolate molecules.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIFDKEDFES FDPELWAAIH AEEIRQQQNI ELIASENIVS KAVMAAQGSV LTNKYAEGYP
70 80 90 100 110 120
GKRYYGGTEA VDVVENLAID RAKELFGAKF ANVQPHSGSQ ANAAAYMALI QPGDTVLGMD
130 140 150 160 170 180
LNAGGHLTHG ASVNFSGKTY HFVPYGVNPQ TELLDYEEIL KIAKEVQPKL IVAGASAYSR
190 200 210 220 230 240
LIDFAKFRQI ADSVGAKLMV DMAHIAGLVA TGAHPNPLPY ADVVTTTTHK TLRGPRGGMI
250 260 270 280 290 300
LTNDEVLAKK INSAIFPGTQ GGPLEHVIAA KAVAFKEALD PEFATYIEQV IKNTQAMADE
310 320 330 340 350 360
FAKVDGLRLI AGGSDNHLLN LKVLDLGING KEAQDLLDSV HITLNKEAIP DETLSPFKTS
370 380 390 400 410
GVRIGAAAIT SRGFKEAEAR KVAQLVSKAL VNHDNQEKLE EVRKSALELT HQFPL