A1RT13 (SYA_PYRIL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine--tRNA ligase
EC=6.1.1.7

Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS

Gene names

Name:	alaS
Ordered Locus Names:	Pisl_0919

Organism

Pyrobaculum islandicum (strain DSM 4184 / JCM 9189) [Complete proteome] [HAMAP]

Taxonomic identifier

384616 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum

Protein attributes

Sequence length	892 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036_A
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A
Subcellular location	Cytoplasm By similarity HAMAP MF_00036_A.
Domain	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. HAMAP MF_00036_A
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 892	892	Alanine--tRNA ligase HAMAP MF_00036_A		PRO_0000347891
Sites
	Metal binding	594	1	Zinc By similarity
	Metal binding	598	1	Zinc By similarity
	Metal binding	702	1	Zinc By similarity
	Metal binding	706	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1RT13 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 5082F1EEE08F12F5	FASTA	892	100,510
	10 20 30 40 50 60 MLSAKVLLNS NFLRKQCPLC KSYFWTRRAD QIYCGDQPCV PYGFIGNPPT KTSIESPAEL 70 80 90 100 110 120 RERFLRFFER NGHVRIKRYP VVARWRDDVY LVGASIYDFQ PWVTSGAVPP PANPLVISQP 130 140 150 160 170 180 SIRLTDVDKV GRSGRHLTGF EMMAHHAFNY PDKYVYWIDE TTQYAYEFFT KELGIPQDEI 190 200 210 220 230 240 TFKESMWEGG GNAGECFEVL VRGLEVATLV FMHYEVKDGK YVELPLKIVD TGYGLERIYW 250 260 270 280 290 300 LLKGTPTIYD AVFSHYLAKV RQKVGIPEPP ADIMGRASIY FGQMDPEVIG LDKAYDIIAE 310 320 330 340 350 360 KIGVDPKWLR EVVRPQEALY VLADHSRTVS WMIADGVIPS NTGAGYLARL LIRRILKNLR 370 380 390 400 410 420 VVGIDAPLVE LFDMHLAELK REYPEIWAAR DLILELVDLE EKKYREVLKS APAAVKKALE 430 440 450 460 470 480 EARRRGRAGL DTDDLVALYD SQGIPPEIVA EVAKSLGAEV KVPDDFYTKL AARHAKREKK 490 500 510 520 530 540 PESPLVEMSK VADLPRTREL FYEDSYMRSF KARVLRVIDG RYVVLDQTAF YPEGGGQPAD 550 560 570 580 590 600 RGVLKFQGGE AKVVDVQRVG HVVVHVVEGQ LPPEGAEVVG EIDWERRYSL MKMHTGTHVL 610 620 630 640 650 660 IQSIRRVLGP HIWQAGAQKD IPSSRLDVTH YKLPTAEEIA KIEELANKVV QENLPVYVKI 670 680 690 700 710 720 MPRNEAEAKY GFILYQGGVV PTREIRVLQI GPDEEPFDIQ ACGGTHLRST GEIGLIKIQK 730 740 750 760 770 780 VERIADGVVR FVFTTGMHAL AYIQELERKL AEAAHIIGGS REEFVESVKK LLQRAEEAER 790 800 810 820 830 840 RAKHYAELYA AVVAENLRAE QIGKYRVAVV ELNDDELAKH IALAATRRDK DLVLVFVGGD 850 860 870 880 890 RVTIYTGGVD VTPVVKTLRE AGFRGGGSKT FAQGLYKGDI QTLKEALKKA LS

References

[1]

"Complete sequence of Pyrobaculum islandicum DSM 4184." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 4184 / JCM 9189.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000504 Genomic DNA. Translation: ABL88095.1.
RefSeq	YP_930438.1. NC_008701.1.
3D structure databases
ProteinModelPortal	A1RT13.
ModBase	Search...
Protein-protein interaction databases
STRING	A1RT13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4617057.
GenomeReviews	Gene locus Pisl_0919 in contig CP000504_GR.
KEGG	pis:Pisl_0919.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04130.
HOGENOM	HBG392147.
OMA	MFTNSGM.
PhylomeDB	A1RT13.
ProtClustDB	PRK13902.
Enzyme and pathway databases
BioCyc	PISL384616:PISL_0919-MONOMER.
Family and domain databases
HAMAP	MF_00036_A. Ala_tRNA_synth_A. [Tree]
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR018162. Ala-tRNA-synth_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR022429. Ala-tRNA_synth_arc. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR03683. A-tRNA_syn_arch. 1 hit. TIGR00344. AlaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_PYRIL

Accession

Primary (citable) accession number: A1RT13

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	February 6, 2007
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program