A8FEH1 (A8FEH1_BACP2) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Asparagine--tRNA ligase HAMAP-Rule MF_00534
EC=6.1.1.22 HAMAP-Rule MF_00534

Alternative name(s):
Asparaginyl-tRNA synthetase HAMAP-Rule MF_00534

Gene names

Name:	asnS HAMAP-Rule MF_00534
Ordered Locus Names:	BPUM_1968

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP] EMBL ABV62638.1

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus pumilus

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). HAMAP-Rule MF_00534 SAAS SAAS004522
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00534
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00534.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. HAMAP-Rule MF_00534 RuleBase RU003746

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP-Rule MF_00534 RuleBase RU003747 SAAS SAAS004522
Cellular component	Cytoplasm HAMAP-Rule MF_00534 SAAS SAAS004522
Ligand	ATP-binding HAMAP-Rule MF_00534 RuleBase RU003747 SAAS SAAS004522 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP-Rule MF_00534 RuleBase RU003747 SAAS SAAS004522 Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP asparagine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A8FEH1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 3D1BE745F2FA4557	FASTA	452	51,740
	10 20 30 40 50 60 MYEKRITPIE KVSFFLALEG IMLKTTINQV FKHVDEDVTI GAWIANKRSS GKIAFLQLRD 70 80 90 100 110 120 GTGFIQGVVV KAEVEEEVFK LAKSVTQETS VYVTGQVTKD ERSPLGFELQ VKSIEVIHEA 130 140 150 160 170 180 TDYPITPKEH GTEFLMDHRH LWLRSKKQHA IMKIRNEIIR ATYEFFHQEG FVKVDPPILT 190 200 210 220 230 240 GSAPEGTTEL FATKYFDEDA YLSQSGQLYM EAAAMALGKV FSFGPTFRAE KSKTKRHLIE 250 260 270 280 290 300 FWMIEPEMAF VEFNENLEYQ ENYVTHVVQS VLENCKVELH TLGRDTAKLE NIKAPFPRIT 310 320 330 340 350 360 YDEAIKFLQE KGFDDIEWGD DFGAPHETAI AESYDKPVFI THYPTSLKPF YMQPAPDRDD 370 380 390 400 410 420 VVLCADLIAP EGYGEIIGGS ERVHDLELLE ARLKEHGLDQ ETYKWYTELR QYGSVPHSGF 430 440 450 GLGLERTVAW ISGAPHVRET IPFPRLLNRL YP

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SAFR-032.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV62638.1.
RefSeq	YP_001487198.1. NC_009848.1.
3D structure databases
ProteinModelPortal	A8FEH1.
ModBase	Search...
Protein-protein interaction databases
STRING	315750.BPUM_1968.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABV62638; ABV62638; BPUM_1968.
GeneID	5621237.
KEGG	bpu:BPUM_1968.
PATRIC	18967836. VBIBacPum16546_2014.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0017.
HOGENOM	HOG000226034.
KO	K01893.
OMA	HEQGFYW.
ProtClustDB	PRK03932.
Enzyme and pathway databases
BioCyc	BPUM315750:GH6N-2057-MONOMER.
Family and domain databases
Gene3D	2.40.50.140. 1 hit.
HAMAP	MF_00534. Asn_tRNA_synth.
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR004522. Asn-tRNA-ligase_IIb. IPR002312. Asp/Asn-tRNA-synth_IIb. IPR012340. NA-bd_OB-fold. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
PANTHER	PTHR22594. PTHR22594. 1 hit. PTHR22594:SF6. PTHR22594:SF6. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMs	TIGR00457. asnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A8FEH1_BACP2

Accession

Primary (citable) accession number: A8FEH1

Entry history

Integrated into UniProtKB/TrEMBL:	November 13, 2007
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)