ID A8V028_9AQUI Unreviewed; 377 AA.
AC A8V028;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
DE Flags: Fragment;
GN ORFNames=HG1285_12342 {ECO:0000313|EMBL:EDP74137.1};
OS Hydrogenivirga sp. 128-5-R1-1.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP74137.1, ECO:0000313|Proteomes:UP000005981};
RN [1] {ECO:0000313|EMBL:EDP74137.1, ECO:0000313|Proteomes:UP000005981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP74137.1,
RC ECO:0000313|Proteomes:UP000005981};
RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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}.
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:EDP74137.1}.
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DR EMBL; ABHJ01000063; EDP74137.1; -; Genomic_DNA.
DR RefSeq; WP_008288396.1; NZ_ABHJ01000063.1.
DR AlphaFoldDB; A8V028; -.
DR PATRIC; fig|392423.7.peg.1295; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000005981; Unassembled WGS sequence.
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; 2.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
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; 2.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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:UP000005981}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDP74137.1"
SQ SEQUENCE 377 AA; 43959 MW; 25771A308D4AFA45 CRC64;
WHALTNKYKD TKDLKENIKQ MIIDWLACGL NPEKATLFVQ SGVKQHAELS LLFSMITPKS
WLELNPSYKD LKFNLFYQYL RDFLLGKQVK INQAPPPENY DNALEKATGK QKNKIFEEYL
RESFHRAFYN QKGINFGYLK EVLIKFGINK KIVEEAVNNL ERGDVGKDID TLGFLAYPVL
QAADILIYKA QGVPVGEDQL PHIELTREIA RRFNNLYGEI FPEPEAILTK EAKLPGIDGR
KMSKSYNNAI YLSDSEEEVN KKTMQMKTDP QRIRRTDPGN PDVCIVYDYH KIFTKDETLL
KDIDNKCRKA EIGCTDCKKI LAENINKFLN PIREKRKEIE KDYEKYEKVF IEGTLKCREI
AENNMKEVRK TMNLYEV
//
