B7J213

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi)
KEGG Pathway
bbz:BbuZS7_0453
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)

87-156 (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 B7J213

Entry ID Method Resolution Chain Position Source
AF-B7J213-F1 Predicted AlphaFoldDB

No variants for B7J213

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B7J213

No associated diseases with B7J213

6 regional properties for B7J213

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 119 - 555 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 19 - 101 IPR004365
domain Aminoacyl-tRNA synthetase, class II 149 - 553 IPR006195
domain GAD domain 309 - 403 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 7 - 135 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 139 - 556 IPR047090

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
MFKVIKCNEL NEKLIDKKVE INAWVKKIRH HGKFIFLNIR DRYEKAQVLV NEEKLLKIAE
70 80 90 100 110 120
KIKLEYCIKI QGLLIKRPPN MINANMKTGH FEILAKNIEI ISKCNELPFM IEDDNNASEN
130 140 150 160 170 180
SKLEYRYLDL RRDSLKNKII LRCQATHLIR NFLIKRKFLE LETPTFVKST PEGARDFVIP
190 200 210 220 230 240
SRIHKGSFYA LPQSPQLYKQ LIMIAGFDKY FQIARCYRDE DSRGDRQPEF TQLDLEMSFV
250 260 270 280 290 300
KKENIFKLIE NMLFLIFKNC ININLPKKFK KITYKKAMNK YGSDKPDTRF ELELQDISRN
310 320 330 340 350 360
LKNSEFNIFK DTLKNKGSIK ILIVKDKADK FSRAKINNLE EIAKLYKTQG LYFTKIENNK
370 380 390 400 410 420
FSGGIAKFLK TEEQELIKTY SLENNDIIFF TANNNWETAC KAMGQIRIKI ANDLGLIDEN
430 440 450 460 470 480
KFEFLWVYDF PLFEYDENTK TYSPAHHMFS LPKKQYIANL EKNPKKTIGE IYDLVLNGVE
490 500 510 520 530 540
LGSGSIRIHN KELQQRIFKI IGFQKEKSED RFGFFLKALE YGAPNHGGIA IGIDRLIMLM
550 560 570 580
TKSTSIKDVI LFPKNSFAAS PLDNSPSKIS NEQLKELGIN IVDGDN