Q5N5I8

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
KEGG Pathway
syc:syc0240_c
EC number
6.1.1.23: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

537-599 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q5N5I8

Entry ID Method Resolution Chain Position Source
AF-Q5N5I8-F1 Predicted AlphaFoldDB

No variants for Q5N5I8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5N5I8

No associated diseases with Q5N5I8

5 regional properties for Q5N5I8

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 152 - 375 IPR000194
domain ATP synthase, alpha subunit, C-terminal 382 - 511 IPR000793
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 29 - 95 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 366 - 375 IPR020003
domain ATP synthase, F1 complex, alpha subunit nucleotide-binding domain 97 - 378 IPR033732

Functions

Description
EC Number 6.1.1.23 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
aspartate-tRNA ligase activity Catalysis of the reaction: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
aspartate-tRNA(Asn) ligase activity Catalysis of the reaction: tRNA(Asx) + L-aspartate + ATP = aspartyl-tRNA(Asx) + diphosphate + AMP.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
nucleic acid binding Binding to a nucleic acid.

1 GO annotations of biological process

Name Definition
aspartyl-tRNA aminoacylation The process of coupling aspartate to aspartyl-tRNA, catalyzed by aspartyl-tRNA synthetase. The aspartyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an aspartic acid 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
MRTHYCGELR AEQVGTSVTL YGWVDRRRDH GGVIFVDLRD RTGTVQIVSD PERTPESYHQ
70 80 90 100 110 120
AEGLRNEYVV KITGRVSGRP AESLNPKLPT GEVEIYADRI EILNAVRRQL PFQVSSADEE
130 140 150 160 170 180
TVREDLRLRY RYLDLRRDRM NRNLQLRHQV VKAIRRFLED EEQFIEIETP VLTKSTPEGA
190 200 210 220 230 240
RDYLVPSRVN PGEWFALPQS PQLFKQLLMV SGFDRYYQIA RCFRDEDLRA DRQPEFTQLD
250 260 270 280 290 300
MEMSFLSQEE IIDLNERLIA HIFKTVKGIE LPRPFPRLTY AEAMDRYGSD RPDTRFGLKL
310 320 330 340 350 360
VDVSDVVADM GFKVFSGAVK SGGKVKILPI PDGNDRISNV RIKPGGDIFK EATEAGAAGL
370 380 390 400 410 420
AYIRVRENGE IDTIGAIKDN LSDEQKAEIL RRTQAQPGTL LLFGAGSTDI VNKSLDRVRQ
430 440 450 460 470 480
FLGKELGLID PEALNLLWVV DFPMVEWNAD EKRYEALHHP FTAPNPQDLE DLTTARAQAY
490 500 510 520 530 540
DIVLNGLEIG GGSLRIYQRD IQERVFETIG LSHEEAQAKF GFLLEAFDFG TPPHGGIAYG
550 560 570 580 590
LDRLVMLLTG EESIRDAIAF PKTQQARCLL TEAPADVSDR QLKELYVAST WQPPIKERD