ID A0A345UKN8_9BACT Unreviewed; 331 AA.
AC A0A345UKN8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN ORFNames=CYPRO_1790 {ECO:0000313|EMBL:AXJ01040.1};
OS Cyclonatronum proteinivorum.
OC Bacteria; Balneolota; Balneolia; Balneolales; Cyclonatronaceae;
OC Cyclonatronum.
OX NCBI_TaxID=1457365 {ECO:0000313|EMBL:AXJ01040.1, ECO:0000313|Proteomes:UP000254808};
RN [1] {ECO:0000313|EMBL:AXJ01040.1, ECO:0000313|Proteomes:UP000254808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Omega {ECO:0000313|EMBL:AXJ01040.1,
RC ECO:0000313|Proteomes:UP000254808};
RA Toshchakov S.V., Korzhenkov A., Samarov N.I., Kublanov I.V., Muntyan M.S.,
RA Sorokin D.Y.;
RT "Phenotypic and genomic properties of Cyclonatronum proteinivorum gen.
RT nov., sp. nov., a haloalkaliphilic bacteroidete from soda lakes possessing
RT Na+-translocating rhodopsin.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
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DR EMBL; CP027806; AXJ01040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345UKN8; -.
DR KEGG; cprv:CYPRO_1790; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000254808; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363036};
KW Reference proteome {ECO:0000313|Proteomes:UP000254808}.
SQ SEQUENCE 331 AA; 37033 MW; 35014F7E47B74570 CRC64;
MSQRSATPVI LSGITPSGRL HAGNYFGAMK QHLEYIEKGE AYYFIANYHA LTSLRDGKLL
EQYTLDVALD YLSLGLDPEK CTFFAQSDVP AVTELAWILG TLCPVSLMEK GVAYKDKVAQ
GLLPNIGLFT YPILQAADIL IYHSDIVPVG ADQKQNLEFA RDLAQKLNNT FEGEYLKLPE
PYIVKDVAIV PGIDGRKMSK SYNNHIFIFD EGKVLKKKVM SIITDATALE DPKNPDTCNV
FSLIKLFATP EKLAEIRAAY LAGGYGYGHA KKELLTLFSD YFAEARERRR ELEKDSDTVR
DILREGGLKA RARAEMVMQP IREVTGIIRT H
//