ID U1PUD4_9EURY Unreviewed; 602 AA.
AC U1PUD4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00140};
DE EC=6.1.1.2 {ECO:0000256|HAMAP-Rule:MF_00140};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140};
DE Short=TrpRS {ECO:0000256|HAMAP-Rule:MF_00140};
GN Name=trpS {ECO:0000256|HAMAP-Rule:MF_00140};
GN ORFNames=J07HQW2_02442 {ECO:0000313|EMBL:ERG95981.1};
OS Haloquadratum walsbyi J07HQW2.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=1238425 {ECO:0000313|EMBL:ERG95981.1, ECO:0000313|Proteomes:UP000030710};
RN [1] {ECO:0000313|EMBL:ERG95981.1, ECO:0000313|Proteomes:UP000030710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HQW2 {ECO:0000313|Proteomes:UP000030710};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC {ECO:0000256|HAMAP-Rule:MF_00140}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00140};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00140}.
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DR EMBL; KE356561; ERG95981.1; -; Genomic_DNA.
DR AlphaFoldDB; U1PUD4; -.
DR STRING; 1238425.J07HQW2_02442; -.
DR eggNOG; arCOG01887; Archaea.
DR HOGENOM; CLU_032621_3_1_2; -.
DR Proteomes; UP000030710; 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:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR HAMAP; MF_00140_A; Trp_tRNA_synth_A; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR InterPro; IPR020653; Tryptophan-tRNA-ligase_arc.
DR PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 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|HAMAP-Rule:MF_00140};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00140}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00140};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00140};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00140}.
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 547..578
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 130..138
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT MOTIF 464..468
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT COMPBIAS 12..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 66264 MW; 8311EE6E81F5B569 CRC64;
MTRDTDDITN ADADPESNTD TNMHTGSNDE TPSEATSSTI TATVVSDGGT AGAEGADDVT
LDPWGSSAVS DYEKLFTEFG IETFDDVLPS VPNPHYLMRR GVVFGHREYG PVAEALRNND
PAAALSGFMP TGDPHIGHKL VFDEIIWHQQ RGADAYALIA DLEAHAARGL TWSEIDEHAR
NYLLSLLALG FDPESGEIYR QSENRKLQNF AFELGSKANF SEFEGIYGFD SETNVAYMQS
VITQMADILY PQLEEPKPTV IPVGPDQDPH VRFARDLAAR MRFFKVTEAY ASFELTDSER
ELVTAVYDER ELYAEDASRP RCAEAATWLT DHLMISTGES GERVEGSENT QDGDTHISID
TVGIVVPDTV VESTIEKLEN AGMEPLRPRV RFLDANATDE AFDALITAIE GEKRRYDEHI
DAFELSAADA TELAREVETN HGGYGFVAPS STYHRFMTGL TGGKMSSSVP ASHISLLDDP
EKGYEKVKAA TTGGRETAEK QRELGGKADE CPVYELFAYL LANDDDLLVT EVYDECVSGD
RLCGNCKEQA AELMQAFLEE HQEKRKEVQS LLDDLDISLT SDRRSIAPGD TTDTDSTDNE
DN
//
