UniProt: A0A0F5EZC2

Database: UniProt
Entry: A0A0F5EZC2_AVIPA

LinkDB:  A0A0F5EZC2_AVIPA 
Original site:  A0A0F5EZC2_AVIPA

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
All databases (14)   

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ID   A0A0F5EZC2_AVIPA        Unreviewed;       302 AA.
AC   A0A0F5EZC2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254,
GN   ECO:0000313|EMBL:RZN56496.1};
GN   ORFNames=EIG79_10200 {ECO:0000313|EMBL:RZN56496.1}, NCTC10926_02666
GN   {ECO:0000313|EMBL:SUV40620.1}, NCTC11296_02589
GN   {ECO:0000313|EMBL:STO72655.1};
OS   Avibacterium paragallinarum (Haemophilus gallinarum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Avibacterium.
OX   NCBI_TaxID=728 {ECO:0000313|EMBL:RZN56496.1, ECO:0000313|Proteomes:UP000294229};
RN   [1] {ECO:0000313|Proteomes:UP000254465, ECO:0000313|Proteomes:UP000254620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10926 {ECO:0000313|EMBL:SUV40620.1,
RC   ECO:0000313|Proteomes:UP000254620}, and NCTC11296
RC   {ECO:0000313|EMBL:STO72655.1, ECO:0000313|Proteomes:UP000254465};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RZN56496.1, ECO:0000313|Proteomes:UP000294229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-3 {ECO:0000313|EMBL:RZN56496.1,
RC   ECO:0000313|Proteomes:UP000294229};
RA   Hellmuth J.E., Boucher C.E., Cason E.D.;
RT   "Sequencing Av. paragallinarum serogroups.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
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DR   EMBL; RQXS01000065; RZN56496.1; -; Genomic_DNA.
DR   EMBL; UGHK01000002; STO72655.1; -; Genomic_DNA.
DR   EMBL; UFSW01000002; SUV40620.1; -; Genomic_DNA.
DR   RefSeq; WP_017806840.1; NZ_VXDA01000039.1.
DR   AlphaFoldDB; A0A0F5EZC2; -.
DR   STRING; 728.VY92_00590; -.
DR   eggNOG; COG0752; Bacteria.
DR   OrthoDB; 9802183at2; -.
DR   Proteomes; UP000254465; Unassembled WGS sequence.
DR   Proteomes; UP000254620; Unassembled WGS sequence.
DR   Proteomes; UP000294229; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   NCBIfam; TIGR00388; glyQ; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00254};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00254};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00254}.
SQ   SEQUENCE   302 AA;  34481 MW;  14BA12958DD608E5 CRC64;
     MSTKFNVKTF QGMILALQEY WANQGCCIVQ PFDMEVGAGT SHPMTALRAI GPEPMAFAYV
     QPSRRPTDGR YGENPNRLQH YYQFQVVIKP SPDNIQELYL GSLKMLGFDP TQHDIRFVED
     NWENPTLGAW GLGWEVWLNG MEVTQFTYFQ QVGGLECKPV TGEVTYGLER LAMYIQGVDS
     VYDLVWSDGP LGKTTYGDVF HQNEVEQSTY NFEYADIDFL FKAFEQYEKE AQELLALEKP
     LPLPAYERIL KAAHSFNLLD ARKAISVTER QRYILRIRAL TKGVAEAYYA SREALGFPGC
     KK
//

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