SYN_ALKOO
ID SYN_ALKOO Reviewed; 463 AA.
AC A8MJ91;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534};
DE EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534};
DE Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534};
GN Name=asnS {ECO:0000255|HAMAP-Rule:MF_00534}; OrderedLocusNames=Clos_2341;
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00534};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00534}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR EMBL; CP000853; ABW19873.1; -; Genomic_DNA.
DR RefSeq; WP_012160180.1; NC_009922.1.
DR AlphaFoldDB; A8MJ91; -.
DR SMR; A8MJ91; -.
DR STRING; 350688.Clos_2341; -.
DR PRIDE; A8MJ91; -.
DR EnsemblBacteria; ABW19873; ABW19873; Clos_2341.
DR KEGG; aoe:Clos_2341; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_9; -.
DR OMA; DNMDLAE; -.
DR OrthoDB; 1138123at2; -.
DR Proteomes; UP000000269; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00457; asnS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..463
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_1000061017"
SQ SEQUENCE 463 AA; 52838 MW; 69FDB59885240AB3 CRC64;
MKSILVKDIY RNTEKYAGQE IVIEGWIRTL RASKAFGFIE VNDGSFFKNI QVVFEEGLEN
FAEVSKLSIS TAIIVKGKLE ITPDAKQPFE IKATSIEVEG ESDSDYPLQK KRHTFEFLRE
IAHLRPRSNT FSAVFRVRSL AAFAIHQFFQ ERGFVYTHTP IITGSDAEGA GEMFRITTLD
PKNPGLNEAG EVDFTKDFFG KETSLTVSGQ LQGEAYALAF RNIYTFGPTF RAENSHTARH
ASEFWMIEPE IAFADLQDNM ELAEEMLKYI INYVMENAPE EMEFFNSFVD KGLLDRLNNV
ATSDFGRVTY TEAIEILQKS GETFEYPVAW GTDLQTEHER YLTEKVFKKP VFVTDYPKDI
KAFYMKLNED GKTVAAMDLL VPGIGEIIGG SQREDNLALL EERMDAMGLD KEEYWWYLEL
RKYGSARHAG YGLGFERAIM YLTGMSNIRD VISFPRTPKS AEF