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Database: UniProt
Entry: A0A1Q8CNY9_9PSEU
LinkDB: A0A1Q8CNY9_9PSEU
Original site: A0A1Q8CNY9_9PSEU 
ID   A0A1Q8CNY9_9PSEU        Unreviewed;       990 AA.
AC   A0A1Q8CNY9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=glyQ {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Synonyms=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   ORFNames=BU204_19075 {ECO:0000313|EMBL:OLF16048.1};
OS   Actinophytocola xanthii.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae.
OX   NCBI_TaxID=1912961 {ECO:0000313|EMBL:OLF16048.1, ECO:0000313|Proteomes:UP000185596};
RN   [1] {ECO:0000313|EMBL:OLF16048.1, ECO:0000313|Proteomes:UP000185596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-183 {ECO:0000313|EMBL:OLF16048.1,
RC   ECO:0000313|Proteomes:UP000185596};
RA   Wang W., Yuan L.;
RT   "The draft genome sequence of Actinophytocola sp. 11-183.";
RL   Submitted (DEC-2016) 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:OLF16048.1}.
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DR   EMBL; MSIE01000034; OLF16048.1; -; Genomic_DNA.
DR   RefSeq; WP_075127100.1; NZ_MSIE01000034.1.
DR   AlphaFoldDB; A0A1Q8CNY9; -.
DR   STRING; 1912961.BU204_19075; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000185596; 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:UP000185596}.
SQ   SEQUENCE   990 AA;  106207 MW;  104273547359A138 CRC64;
     MQDALLALTR YWTDRGCMIV QPFNTEVGAG TLNPATILRV LGPEPWRVAY VEPSVRPDDS
     RYGENPNRLQ THTQFQVILK PDPGDPQEQY LASLEALGID IHAHDIRFVE DNWANPATGS
     WGLGWEVWLD GLEITQFTYF QQAGGMSLDP VSVEITYGVE RIIMALQGVS HFKDIQYAPG
     ISYGEAFGQA EYEMSRFYLD DADVDTQRRL FEDYAAEARR LLDARLPVPA HVHVLKCSHT
     FNVLDARGAV STTERARAFA RMRALAREVS ALWAQRREEL GHPLGLTPAL SAAAPAESLP
     EVSAAAPLLF EIGTEELPPG EVTRSARAVR EALTAKLAGT RLEHGAVEVH ATPRRIVVVV
     EEVAPREPDA ERFVRGPRVS AAFDADGNPT KAAAGFARGQ GVEVSALERV EVDGVEHVGV
     TRTDAGRGAV EVLAEVLGSL VAELRADKNM RWNDPKLSFT RPVRWLVALL GSEVVPVVAS
     SLAAGRTTRV HRTAESPVVE VPSASGYLDF LASHGIVASP SARRATIVSA ATALAESVGG
     RIDVEGEAAL LDEITNLVEE PNAILGGFAP SYLDLPQEIL TTVMRKHQRY VPVRDAEGNL
     LPHFVAVANG SCAADAVRAG NEAVLRARYE DASFFWRADL QVAPEAMKSG LARLAFEERL
     GSMADRAARI AAVAGNLGSA LSSADRATLD RAAVLAKFDL GSQMVIELTS LAGVMAREYA
     VRAGETPEVA QALFDMERPR SAGDAAPATV PGAVLALADR FDMLVGLFAV GAAPTGSSDP
     FGLRRAASGV ITILRAHPSL REITFERGLA AAAQHVRAQG IEVAEATLAE AAEFITRRQE
     QQLLDAGHDH RHVAAVLALP PATAAETLAE IESRQGNEEF AALAAALQRV RRIVPADTAP
     SYDTARLTEP AEVALHQALV KVADSLGAGP HSLAHFADVA SALTEPINTF FDEILVMAED
     PEVRAARLGL LATIRDLAAP TLDWQALGTQ
//
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