ID H5UW15_9MICO Unreviewed; 1035 AA.
AC H5UW15;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|HAMAP-Rule:MF_00255};
DE Includes:
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
DE Includes:
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
GN Name=glyQS {ECO:0000313|EMBL:GAB49923.1};
GN Synonyms=glyQ {ECO:0000256|HAMAP-Rule:MF_00254}, glyS
GN {ECO:0000256|HAMAP-Rule:MF_00255};
GN ORFNames=MOPEL_135_01610 {ECO:0000313|EMBL:GAB49923.1};
OS Mobilicoccus pelagius NBRC 104925.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Mobilicoccus.
OX NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB49923.1, ECO:0000313|Proteomes:UP000004367};
RN [1] {ECO:0000313|EMBL:GAB49923.1, ECO:0000313|Proteomes:UP000004367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB49923.1,
RC ECO:0000313|Proteomes:UP000004367};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925.";
RL Submitted (FEB-2012) 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_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB49923.1}.
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DR EMBL; BAFE01000094; GAB49923.1; -; Genomic_DNA.
DR AlphaFoldDB; H5UW15; -.
DR STRING; 1089455.MOPEL_135_01610; -.
DR eggNOG; COG0751; Bacteria.
DR eggNOG; COG0752; Bacteria.
DR Proteomes; UP000004367; 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 HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR NCBIfam; TIGR00388; glyQ; 1.
DR NCBIfam; TIGR00211; glyS; 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 Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 2.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00255};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00255};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000004367}.
SQ SEQUENCE 1035 AA; 111932 MW; B5B3DB9C80BE1459 CRC64;
MQDALRKLSD YWTSRGCLTW QPFNTEVGAG TMNAATVLRV LGPEPWDVAY VEPSVRPDDS
RYGENPNRLQ THTQFQVILK PEPGDPQELY LGSLEALGID LDAHDVRFVE DNWQQPAIGA
WGLGWEVWLD GMEITQFTYF QQVGGQDLDP IPVELTYGME RILMAQQGVT HFKDIVYAIK
PDGTPITYGE TFGQNEYEMS RYYLDDADVE ANQRLYETFV AEATRMVEAR LPVPAHQYIL
KSSHAFNVLD ARGAISTTER AQAFATMRRL MRDTAALWVE RRKELGFPLL KDADAQEAPA
AEASTDAVTE APEIAADAAP QTFALEIGVE ELPPHVLPQT VEAVREALTS GLAATRLEHG
TITVDGTPRR VVAVVEGVAA REPDATQLRK GPKWAAAFDA DGNLTKPLEG FMRGQGVTRD
QVVKAEIGGN EHACVEIDVP GRDAVTVLGG IVESCVKGLR AEKNMRWSDP ALSFSRAVRW
LVALWGDVVV PAQISEVHAG RTTYLQRVTE ASRGADGRSG RRADGAPVGH VEVTSADELL
TAIERGEIEW RTADRRADVV RQATALAEAE GGRIDVDANA DLLDEITNLV EQPHGILGRF
DERYLELPDR ILTSVMARHQ RYLPVLDAQG DLMPCFVTMA NGTCDDDVVR AGNESVIRAR
YEDALFFWNA DLQAGTVDEF VPGLDTLTFE NRLGSVGQRA RRIAAVASAL GDAVALDAQE
RETLTRAGQL AKFDLATQLV VEMSSLAGFV AREYALRKGE PEAVAQALYE MEQPHTAVDA
VPASVSGALL ALGDRFDLLM AMFALGAKPT GSSDPYGLRR AALGVVRILR EAHAGGPLAP
LSGVTVTDGL TAAAARLREQ GITVSDDAVA SAAEFTTGRL AQLLRDEGVG ADLVATVLPA
ADRPGSLAQA LADVTTLREG DRADELEALV EALVRIERIV PAGTAATYDA ALLTEPAEVE
LRESLERLAS HDDLPGYLAA VGDAGLVPAI ARFFDDILVM AKEEDVKAAR LGLLAAVRAT
APTGIDYRAL DTLLA
//
