A1RWQ1 (SYA_THEPD) 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:	Tpen_0221

Organism

Thermofilum pendens (strain Hrk 5)

Taxonomic identifier

368408 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermofilaceae › Thermofilum

Protein attributes

Sequence length	907 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 Reference 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 – 907	907	Alanine--tRNA ligase HAMAP MF_00036_A		PRO_1000074515
Sites
	Metal binding	602	1	Zinc By similarity
	Metal binding	606	1	Zinc By similarity
	Metal binding	706	1	Zinc By similarity
	Metal binding	710	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1RWQ1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 4B473AE5FCBC8563	FASTA	907	102,487
	10 20 30 40 50 60 MSKEDFVNLP FFVENGWIKR TCPVCGRTFW TLDPERKVCG DQPCEEYSFI GRSVGVKPES 70 80 90 100 110 120 LSATRKMFID FFEKRNHTPV KRYPVVARWR EDVYLVGASI YDFQPWVTEG LVPPPANPLV 130 140 150 160 170 180 ISQPSIRLTD LDNVGKTGRH LTGFEMMAHH AFNIRDQRVY WANETVEYAF EVLTKVYGVK 190 200 210 220 230 240 PEEITFIFDM WSGGGNAGED YEVIVRGLEV ATLVFMHYKT AEDGSLIPIE NRIVDTGYGL 250 260 270 280 290 300 ERIYWLLTGH YNVYEAVFSG VIDRLRKLSG VEKPPDDLMY RLALKSGRLD FKKPLEALET 310 320 330 340 350 360 LRNVSREVGI SFEELQRVLE PNEALYALAD HTRTIAWMLG DGVVPSNSGA GYLARLLIRR 370 380 390 400 410 420 SLRLLRRLQL ELPLSEIVLW QIQYWRNDFP EYLELQDEIR DIVDTEEERF EESVKRGEKV 430 440 450 460 470 480 LGALLGELKS KGLRVVPAEE IVKLYESHGV PPELVKEKAE SEGLEADITG FYSRLAEMRS 490 500 510 520 530 540 RAQVQQKEAL QLPLDPSRLK EFRPTRLLYY ENEKLAEFEA TVLGVLDGKY VVLDSTAFYP 550 560 570 580 590 600 EGGGQLSDTG VLVYEGGECR VKYAFKVGDI VVHECEGNAP PVGARVKGVV DMERRLALMR 610 620 630 640 650 660 HHTATHIVLG ALRSVLGKHV WQAGAQKTPD YVRFDFTHHK AITPEQAKAI EALANRVVME 670 680 690 700 710 720 DRPVRKYLLN RTEAEKAFGF TLYQGGAVPQ TTLRVVEIPG WDAEACGGTH CDRTGEIGLI 730 740 750 760 770 780 KILGFEKIQD GVVRVVFKAG MPALEYVQGM GDKLKNLQEI LDASYEGLEE KAKSLKSRIE 790 800 810 820 830 840 ALEKEVKKLR EELLKGGVSV SPVATVQGVQ VYVYFSDEYE PREAALAISR TRTSSVILAY 850 860 870 880 890 900 NSKGNFALKV TDDLLDRLDA REIGRSVCES LRGKGGGVRD LYQGRIDETK SVDKVIVEAL RQALERR

References

[1]

"Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction." Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B. , Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N. J. Bacteriol. 190:2957-2965(2008) [PubMed: 18263724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hrk 5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000505 Genomic DNA. Translation: ABL77631.1.
RefSeq	YP_919634.1. NC_008698.1.
3D structure databases
ProteinModelPortal	A1RWQ1.
ModBase	Search...
Protein-protein interaction databases
STRING	A1RWQ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4601814.
GenomeReviews	Gene locus Tpen_0221 in contig CP000505_GR.
KEGG	tpe:Tpen_0221.
Phylogenomic databases
eggNOG	arNOG04130.
HOGENOM	HBG392147.
OMA	MFTNSGM.
PhylomeDB	A1RWQ1.
ProtClustDB	PRK13902.
Enzyme and pathway databases
BioCyc	TPEN368408:TPEN_0221-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. IPR024796. T4_endonuc_V_domain. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
Gene3D	G3DSA:1.10.440.10. Pyr_DNA_glycsyls. 1 hit.
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. SSF47077. Pyr-dimer_DNA_glycosylase. 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_THEPD

Accession

Primary (citable) accession number: A1RWQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 6, 2007
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program