UniProt: A0A2C9CV38

Database: UniProt
Entry: A0A2C9CV38_9RHOB

LinkDB:  A0A2C9CV38_9RHOB 
Original site:  A0A2C9CV38_9RHOB

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
All databases (14)   

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ID   A0A2C9CV38_9RHOB        Unreviewed;       763 AA.
AC   A0A2C9CV38;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=SAMN06273572_11032 {ECO:0000313|EMBL:SOH95361.1};
OS   Monaibacterium marinum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Monaibacterium.
OX   NCBI_TaxID=1690039 {ECO:0000313|EMBL:SOH95361.1, ECO:0000313|Proteomes:UP000220034};
RN   [1] {ECO:0000313|EMBL:SOH95361.1, ECO:0000313|Proteomes:UP000220034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 {ECO:0000313|EMBL:SOH95361.1,
RC   ECO:0000313|Proteomes:UP000220034};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-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}.
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DR   EMBL; OCTN01000010; SOH95361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C9CV38; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000220034; 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          649..754
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   763 AA;  82988 MW;  9B00939169AAE8D5 CRC64;
     MSDLLIELFS EEIPARMQAK AADDLRRLMT DGMVEAGLTY AGAAAFATPR RLTLAVEGLT
     TESPTLREER KGPRTDAPEK ALAGFLRSTG LTKEQLEVRD DKKGQVYFAV VEKPGRAAAD
     IVAEVLEKAI RTFPWPKSMR WGTGTLRWVR PLHSILAILS DEEGAQVVPL DVDGIASGDT
     THGHRFMAPD VIKVTSFEDY AAKLKRAFVI LDPQERADLI HAEATNMAFA QGLEIVEDKG
     LLAEVAGLVE WPVPLMGPIG EQFLELPPEV LQTSMKEHQK FFSVRDPATG KIVKYVTVAN
     RQTTDNGATI LAGNSKVLTA RLSDAKFFWE NDLQTVRERG LEGMAAPLAN VTFHNKLGSQ
     AERIERIAAL AREIAPLVGA DADMAEQAAK IAKADLSSEM VYEFPELQGL MGRYYAEAAG
     LPQPVANAAQ LHYSPLGPSD DVPTEPVSVA VALADKLDTL TGFWAIDEKP TGSKDPYALR
     RAALGVIRLV LGSEVRTDLS EVLLTHGREI LAIKSKLDSA YEAEVIAGAA QEKLLEAQTE
     VLATASGANK EKLKQIAVNL SAQYNDAQQN HSLLLNKANE ASQSACCIPP LLLEFFADRL
     KVHLRGEGIR HDVIDAALPE NWDGDIVLLV NRVRALQSFL DTEDGANLLA AYTRASNIVK
     AEEGKDGVEY SLDPNPDLAE NDSEKALFAA LDAADPQIDA ALKAEDFAAA MGAIAALRSS
     LDTYFEATLI NSENQIIRRN RLCLLNRIRN LFARIADFAK LDG
//

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