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Database: UniProt
Entry: A0A258NZH2_9BURK
LinkDB: A0A258NZH2_9BURK
Original site: A0A258NZH2_9BURK 
ID   A0A258NZH2_9BURK        Unreviewed;       709 AA.
AC   A0A258NZH2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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};
GN   Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   ORFNames=B7Y60_11170 {ECO:0000313|EMBL:OYY35726.1};
OS   Polaromonas sp. 35-63-35.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1970418 {ECO:0000313|EMBL:OYY35726.1, ECO:0000313|Proteomes:UP000216365};
RN   [1] {ECO:0000313|EMBL:OYY35726.1, ECO:0000313|Proteomes:UP000216365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35-63-35 {ECO:0000313|EMBL:OYY35726.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       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:OYY35726.1}.
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DR   EMBL; NCFQ01000008; OYY35726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258NZH2; -.
DR   Proteomes; UP000216365; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
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; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 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_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}.
FT   DOMAIN          601..699
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   709 AA;  76105 MW;  FF10B91AE19DBE2C CRC64;
     MTTQNLLVEL FVEELPPKAL KKLGEAFAGV LFEQLKAQGL ASADTSVVTA YASPRRLAAH
     VTHVWRKAAD KAVQQKLMPV SVGLDASGNA TPALLKKLQA LGADVSDPAA AVAALKRAPD
     GKAEALFYDS LVTGATLDTG LQKALEEAIA KLPIPKVMSY QLETDCALPG WSSVNFVRPA
     HGLVALHGST VVPITALGLK AGNTTQGHRF EAKVSPVVIK DADAYAQTLL SDGAVIASFD
     DRRFAIVQQL AQAAERLGPG YEVLMDEDLL SEVTGLVEHP NVLVCAFESQ FLDVPQECLI
     LTMKANQKYF PLVDAKGKLT NKFLVVSNIS PDDASAVIGG NERVVRPRLA DAKFFFDQDR
     KKTLASRVAG LDKVVYHNKL GSQGERVQRV RTIAEAIANR LNANVADVQR AAELAKTDLV
     TDMVGEFPEL QGIMGRYYAL NDGLSAEVAD AIEDHYKPRF AGDELPRNTI GVMVALADKL
     ETLVGMFGIG NLPTGDKDPF ALRRHALGVI RMLVEKDLPL GLAELVEDAT PVFGDKITNA
     SAALTDFIYD RLAGSLREQG FSAQEVEAVL ALRPQRLGDV AKRLAAVRAF AALPEAPALA
     AANKRISNIL KKAQDVDAHV SEVLLKEPAE VALYAAMQEL APKANSQFEA GDYTASLQTL
     AALRAPVDAF FDGVMVNAEE MDLRLNRQGL LKSLHDAMNR VADLSKLAS
//
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