UniProt: Q31Q07

Database: UniProt
Entry: Q31Q07_SYNE7

LinkDB:  Q31Q07_SYNE7 
Original site:  Q31Q07_SYNE7

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
All databases (20)   

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ID   Q31Q07_SYNE7            Unreviewed;       462 AA.
AC   Q31Q07;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Asparagine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00534};
DE            EC=6.1.1.22 {ECO:0000256|HAMAP-Rule:MF_00534};
DE   AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00534};
DE            Short=AsnRS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   Name=asnS {ECO:0000256|HAMAP-Rule:MF_00534};
GN   OrderedLocusNames=Synpcc7942_0830 {ECO:0000313|EMBL:ABB56862.1};
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB56862.1, ECO:0000313|Proteomes:UP000889800};
RN   [1] {ECO:0000313|Proteomes:UP000889800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC   {ECO:0000313|Proteomes:UP000889800};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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:0000256|HAMAP-Rule:MF_00534};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00534}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00534}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00534}.
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DR   EMBL; CP000100; ABB56862.1; -; Genomic_DNA.
DR   RefSeq; WP_011377750.1; NZ_JACJTX010000005.1.
DR   AlphaFoldDB; Q31Q07; -.
DR   STRING; 1140.Synpcc7942_0830; -.
DR   PaxDb; 1140-Synpcc7942_0830; -.
DR   GeneID; 76399580; -.
DR   KEGG; syf:Synpcc7942_0830; -.
DR   eggNOG; COG0017; Bacteria.
DR   HOGENOM; CLU_004553_2_0_3; -.
DR   OrthoDB; 9762036at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_0830-MONOMER; -.
DR   Proteomes; UP000889800; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00776; AsxRS_core; 1.
DR   CDD; cd04318; EcAsnRS_like_N; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   NCBIfam; TIGR00457; asnS; 1.
DR   PANTHER; PTHR22594:SF34; ASPARAGINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00534};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00534}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00534};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00534};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00534};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00534}; Reference proteome {ECO:0000313|Proteomes:UP000889800}.
FT   DOMAIN          135..452
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   462 AA;  52262 MW;  49B78E3F7413E232 CRC64;
     MASARIVDLL SQGQPGQTVV VRGWIRTARQ LKEFTFVEVN DGSCLKGIQV VLGQELADYE
     MLAKQLDTGA AIAVEGQLVA SPAKGQRVEL QAASVEIVGG ADPEQYPLQK KRHSFEFLRT
     IAHLRPRTNS LGAVMRVRNA AATAIHDFFQ ERGFLWVHTP IITASDCEGA GELFTVTNLD
     LDKLGQSQQA PDFEQDFFGK RAYLTVSGQL EAEIMALAFS NVYTFGPTFR AENSNTSRHL
     AEFWMVEPEM AFCDLGGDMD LAEAFLKFVF QRVSDRCSED LEFFNQRIDS EVLNRAETIL
     NNDFERVSYT DAIALLEKAD RSFDYPVAWG IDLQSEHERY LAEEYFRKPL IVYDYPREIK
     AFYMRLNDDQ KTVAAMDVLA PGIGEIIGGS QREERLDVLK QRLAEANLPE ENYWWYLDLR
     RYGSVPHAGF GLGFERLVQF ITGMGNIRDV IPFPRTPQNA EF
//

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