(data stored in ACNUC7421 zone)

SWISSPROT: A8FP55_SHESH

ID   A8FP55_SHESH            Unreviewed;       287 AA.
AC   A8FP55;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 62.
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   OrderedLocusNames=Ssed_0015 {ECO:0000313|EMBL:ABV34628.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34628.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34628.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34628.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly). {ECO:0000256|HAMAP-Rule:MF_00254,
CC       ECO:0000256|SAAS:SAAS00392644}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|SAAS:SAAS00514589}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254,
CC       ECO:0000256|SAAS:SAAS00392629}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00254,
CC       ECO:0000256|SAAS:SAAS00578611}.
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DR   EMBL; CP000821; ABV34628.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8FP55; -.
DR   STRING; 425104.Ssed_0015; -.
DR   EnsemblBacteria; ABV34628; ABV34628; Ssed_0015.
DR   KEGG; sse:Ssed_0015; -.
DR   eggNOG; COG0752; LUCA.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; LGSYYQF; -.
DR   OrthoDB; POG091H01SB; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   TIGRFAMs; TIGR00388; glyQ; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FP55.
DR   SWISS-2DPAGE; A8FP55.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00104890};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514602};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514628};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514596, ECO:0000313|EMBL:ABV34628.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514600};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514587}.
SQ   SEQUENCE   287 AA;  32762 MW;  0D4312A1E5CE9C7A CRC64;
     MTLQEFWAQQ GCAIVQPLDM EVGAGTFHPM TFLRALGPEP MSCAYVQPSR RPTDGRYGDN
     PNRLQHFYQF QVVLKPSPDN IQELYLGSLA AAGIDMDIHD VRFVEDNWES PTLGAWGLGW
     EVWLNGMEVS QFTYFQQVGG LECKPVTGEI TYGLERLAMY IQEVDNVYDL VWTDGPMGKV
     MYGDIFHQNE VEQSAYNFEH ANVEVLFRTF DDCEKACQHL LNLEKPLPLP AYEQVMKASH
     AFNLLDARHA ISVTERQRYI LRVRTMAKGV AESYYQAREA LGFPICK
//

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