C5CCH2

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus)
KEGG Pathway
mlu:Mlut_12790
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)

327-396 (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 C5CCH2

Entry ID Method Resolution Chain Position Source
AF-C5CCH2-F1 Predicted AlphaFoldDB

No variants for C5CCH2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C5CCH2

No associated diseases with C5CCH2

6 regional properties for C5CCH2

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 119 - 560 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 18 - 101 IPR004365
domain Aminoacyl-tRNA synthetase, class II 142 - 557 IPR006195
domain GAD domain 309 - 409 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 2 - 135 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 139 - 560 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
MLRTHSLGEL NASLIGQTVT VTGWVARRRD HGGVAFVDLR DASGFAQVVV RDEADFDPLR
70 80 90 100 110 120
NEWVLQVTGT VERRPEGNEN PNLPSGEIEL IAETVTVLNT AAALPFQVDE HVEVGEEARL
130 140 150 160 170 180
RHRYLDLRRP QPSRIMRLRS EVNRTARELL HGEGFVEVET PTLTRSTPEG ARDFLVPARL
190 200 210 220 230 240
APGSWYALPQ SPQLFKQLLQ VGGIEKYYQI ARCYRDEDFR ADRQPEFTQL DIEASFVEQD
250 260 270 280 290 300
DVIALGEKIV KALWALVGVD VPTPIRRMTY AEAMEKYGSD KPDLRFGLEL TDLTEYFKDT
310 320 330 340 350 360
PFRVFQNEYV GAVVMPGGAS QARRTLDAWQ EWAKQRGAKG LAYVLIQEDG ELTGPVSKNI
370 380 390 400 410 420
SEEEKAGLAA AVGANPGDCV FFAAGKPKES RALLGAARVE IGRRCGLFTD AGDGVAAKDA
430 440 450 460 470 480
DWAFVWVVDA PMFEPAADAV ASGDVAVGAG AWTAVHHAFT SPKPEFADTF DADPGSALAY
490 500 510 520 530 540
AYDIVCNGNE IGGGSIRIHR RDVQERVFEV MGLSPEEANE KFGFLLEGFK YGAPPHGGIA
550 560 570 580 590 600
FGWDRVVALL AGTDSIREVI AFPKTGGGFD PLTGAPAPIT AQQRKEAGVD AQPEPKQAEA
EPEA