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Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Edits incorrectly charged Ser-tRNA(Ala). Incorrectly charged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Gly and Ser) in the charging step.1 Publication

Catalytic activityi

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi613Zinc1
Metal bindingi617Zinc1
Metal bindingi717Zinc1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

Enzyme and pathway databases

BRENDAi6.1.1.7. 5244.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase (EC:6.1.1.7)
Alternative name(s):
Alanyl-tRNA synthetase
Short name:
AlaRS
Gene namesi
Name:alaS
Ordered Locus Names:PH0297
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi633Q → M: Significant deacylation of correctly charged L-alanyl-tRNA(Ala) occurs. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000752741 – 915Alanine--tRNA ligaseAdd BLAST915

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi70601.PH0297.

Structurei

Secondary structure

1915
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 12Combined sources5
Beta strandi16 – 19Combined sources4
Turni21 – 23Combined sources3
Beta strandi26 – 30Combined sources5
Turni40 – 42Combined sources3
Beta strandi48 – 50Combined sources3
Beta strandi52 – 55Combined sources4
Helixi59 – 71Combined sources13
Beta strandi74 – 76Combined sources3
Helixi100 – 104Combined sources5
Turni105 – 111Combined sources7
Beta strandi116 – 127Combined sources12
Helixi132 – 134Combined sources3
Turni135 – 137Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi143 – 154Combined sources12
Helixi163 – 176Combined sources14
Helixi182 – 184Combined sources3
Beta strandi185 – 189Combined sources5
Beta strandi192 – 194Combined sources3
Beta strandi197 – 199Combined sources3
Beta strandi201 – 206Combined sources6
Beta strandi209 – 221Combined sources13
Beta strandi231 – 233Combined sources3
Turni234 – 236Combined sources3
Beta strandi237 – 252Combined sources16
Helixi253 – 261Combined sources9
Helixi266 – 270Combined sources5
Helixi272 – 282Combined sources11
Helixi289 – 300Combined sources12
Beta strandi304 – 308Combined sources5
Helixi310 – 321Combined sources12
Helixi325 – 353Combined sources29
Beta strandi359 – 361Combined sources3
Helixi362 – 380Combined sources19
Helixi387 – 398Combined sources12
Turni399 – 401Combined sources3
Helixi404 – 407Combined sources4
Helixi409 – 444Combined sources36
Helixi451 – 461Combined sources11
Helixi465 – 472Combined sources8
Turni474 – 476Combined sources3
Helixi485 – 490Combined sources6
Helixi491 – 494Combined sources4
Beta strandi507 – 513Combined sources7
Helixi519 – 522Combined sources4
Beta strandi528 – 537Combined sources10
Beta strandi540 – 546Combined sources7
Beta strandi560 – 564Combined sources5
Beta strandi567 – 577Combined sources11
Beta strandi580 – 586Combined sources7
Helixi588 – 590Combined sources3
Beta strandi596 – 601Combined sources6
Helixi603 – 627Combined sources25
Beta strandi632 – 638Combined sources7
Beta strandi643 – 648Combined sources6
Helixi655 – 671Combined sources17
Beta strandi674 – 681Combined sources8
Helixi682 – 689Combined sources8
Helixi691 – 693Combined sources3
Beta strandi695 – 697Combined sources3
Beta strandi701 – 709Combined sources9
Turni710 – 712Combined sources3
Beta strandi713 – 716Combined sources4
Helixi725 – 728Combined sources4
Beta strandi731 – 740Combined sources10
Beta strandi743 – 750Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZZEX-ray2.16A/B1-752[»]
2ZZFX-ray2.70A1-752[»]
2ZZGX-ray3.10A/B1-752[»]
ProteinModelPortaliO58035.
SMRiO58035.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58035.

Family & Domainsi

Domaini

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs (By similarity).By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG01255. Archaea.
COG0013. LUCA.
HOGENOMiHOG000015496.
KOiK01872.
OMAiLDVTHYK.

Family and domain databases

HAMAPiMF_00036_A. Ala_tRNA_synth_A. 1 hit.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR022429. Ala-tRNA_lgiase_arc.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O58035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFIMKTRMF EEEGWIRKKC KVCGKPFWTL DPDRETCGDP PCDEYQFIGK
60 70 80 90 100
PGIPRKYTLD EMREKFLRFF EKHEIYPHGR VKRYPVLPRW RDDVLLVGAS
110 120 130 140 150
IMDFQPWVIS GEADPPANPL VISQPSIRFT DIDNVGITGR HFTIFEMMAH
160 170 180 190 200
HAFNYPGKPI YWMDETVELA FEFFTKELKM KPEDITFKEN PWAGGGNAGP
210 220 230 240 250
AFEVLYRGLE VATLVFMQYK KAPENAPQDQ VVVIKGEKYI PMETKVVDTG
260 270 280 290 300
YGLERLVWMS QGTPTAYDAV LGYVVEPLKK MAGIEKIDEK ILMENSRLAG
310 320 330 340 350
MFDIEDLGDL RYLREQVAKR VGITVEELEK AIRPYELIYA IADHTKALTF
360 370 380 390 400
MLADGVVPSN VKAGYLARLL IRKSIRHLRE LGLEVPLSEI VALHIKELHK
410 420 430 440 450
TFPEFKEMED IILEMIELEE KKYAETLRRG SDLVRREIAK LKKKGIKEIP
460 470 480 490 500
VEKLVTFYES HGLTPEIVKE IAEKEGVKVN IPDNFYSMVA KEAERTKEEK
510 520 530 540 550
GEELVDFELL KDLPDTRRLY YEDPFMKEFD AKVLRVIKDW VILDATAFYP
560 570 580 590 600
EGGGQPYDTG VLIVNGREVK VTNVQKVGKV IIHKVEDPGA FKEGMIVHGK
610 620 630 640 650
IDWKRRIQHM RHHTGTHVLM GALVRVLGRH VWQAGSQLTT DWARLDISHY
660 670 680 690 700
KRISEEELKE IEMLANRIVM EDRKVTWEWL PRTTAEQKYG FRLYQGGVVP
710 720 730 740 750
GREIRVVKIE DWDVQACGGT HLPSTGLVGP IKILRTERIQ DGVERIIFAC
760 770 780 790 800
GEAAIREWQK ERDLLKKASN VLRVPPEKLP ETAERFFNEW KEARKEVDKL
810 820 830 840 850
KKELARLLVY ELESKMQKIG SIEFIGEVVE GSMEDLRELV EKLKKPKRVV
860 870 880 890 900
VLISRDGYFA VSVGSEVGVE ANELAKKITL IAGGGGGGRR DIAQGKVKDI
910
SKAKDVIESI KSMFS
Length:915
Mass (Da):105,011
Last modified:August 1, 1998 - v1
Checksum:iAFD4C26939928D33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29370.1.
PIRiC71455.
RefSeqiWP_010884393.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA29370; BAA29370; BAA29370.
GeneIDi1444180.
KEGGipho:PH0297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29370.1.
PIRiC71455.
RefSeqiWP_010884393.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZZEX-ray2.16A/B1-752[»]
2ZZFX-ray2.70A1-752[»]
2ZZGX-ray3.10A/B1-752[»]
ProteinModelPortaliO58035.
SMRiO58035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA29370; BAA29370; BAA29370.
GeneIDi1444180.
KEGGipho:PH0297.

Phylogenomic databases

eggNOGiarCOG01255. Archaea.
COG0013. LUCA.
HOGENOMiHOG000015496.
KOiK01872.
OMAiLDVTHYK.

Enzyme and pathway databases

BRENDAi6.1.1.7. 5244.

Miscellaneous databases

EvolutionaryTraceiO58035.

Family and domain databases

HAMAPiMF_00036_A. Ala_tRNA_synth_A. 1 hit.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR022429. Ala-tRNA_lgiase_arc.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYA_PYRHO
AccessioniPrimary (citable) accession number: O58035
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Unlike the case in Archaeoglobus fulgidus and some of the free-standing tRNA(Ala) AlaX editing proteins, His-721 does not bind zinc but forms a hydrogen bond with Cys-717 instead.Curated

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.