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 Q2SJB8

Entry ID Method Resolution Chain Position Source
AF-Q2SJB8-F1 Predicted AlphaFoldDB

No variants for Q2SJB8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2SJB8

No associated diseases with Q2SJB8

2 regional properties for Q2SJB8

Type Name Position InterPro Accession
domain IRS-type PTB domain 13 - 115 IPR002404
domain FRS2, PTB domain 15 - 106 IPR038742

Functions

Description
EC Number 6.1.1.11 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.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
serine-tRNA ligase activity Catalysis of the reaction: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).

3 GO annotations of biological process

Name Definition
selenocysteine biosynthetic process The chemical reactions and pathways resulting in the formation of selenocysteine, an essential component of glutathione peroxidase and some other proteins.
selenocysteinyl-tRNA(Sec) biosynthetic process The chemical reactions and pathways resulting in the formation of selenocysteinyl-tRNA(Sec). This process occurs through the following steps: a unique serine-tRNA with a UGA recognizing anticodon is first aminoacylated with serine; this is then phosphorylated by phosphoseryl-tRNA
seryl-tRNA aminoacylation The process of coupling serine to seryl-tRNA, catalyzed by seryl-tRNA synthetase. The seryl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a serine-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
MLDPKLLRNS LDEVAARLKT KRYDLDVDAF SQLEERRKSV QVRTEELQSE RNSKSKNIGM
70 80 90 100 110 120
MIKQGQDPQP LKDEVAKIGE QLETAKAELQ DIQDKLDDLL QGIPNLPDAS VPEGASEDDN
130 140 150 160 170 180
VEVRQWGSVR EFDFEPKDHV DLGESLGLLD FNSGAKLAGS RFVVMRRELA RLHRALAQFM
190 200 210 220 230 240
LDIHTTEHGY QETMTPFLVH AHALQGTGQL PKFEADLFKV PGEHDFYLIP TAEVPVTNLV
250 260 270 280 290 300
REEILDAKEL PLKMTSHTPC FRSEAGSYGR DVRGMIRQHQ FEKVELIHVV APEQSDAALE
310 320 330 340 350 360
ELTGNAERIL QLLNLPYRVV ALCGGDLGFS AAKTYDIEVW LPAQKKYREI SSCSNCRDFQ
370 380 390 400 410 420
ARRMQARWRN PETGKPELVH TLNGSGLAIG RTLIAVLENY QQADGSILVP DVLEPYMGGV
KVIKSAN