ID D3SUL2_NATMM Unreviewed; 570 AA.
AC D3SUL2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=trpS1 {ECO:0000313|EMBL:ADD05270.1};
GN Synonyms=trpS {ECO:0000256|HAMAP-Rule:MF_00140};
GN OrderedLocusNames=Nmag_1694 {ECO:0000313|EMBL:ADD05270.1};
GN ORFNames=C500_11885 {ECO:0000313|EMBL:ELY29008.1};
OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS magadii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD05270.1, ECO:0000313|Proteomes:UP000001879};
RN [1] {ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000001879};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA Maupin-Furlow J.A., Woyke T.;
RT "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADD05270.1, ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD05270.1}, and ATCC 43099 / DSM
RC 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT "A comparative genomics perspective on the genetic content of the
RT alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL BMC Genomics 13:165-165(2012).
RN [3] {ECO:0000313|EMBL:ELY29008.1, ECO:0000313|Proteomes:UP000011543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC {ECO:0000313|EMBL:ELY29008.1};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:ADD05270.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD05270.1};
RA Pfeiffer F.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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,
CC ECO:0000256|RuleBase:RU363036}.
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DR EMBL; CP001932; ADD05270.1; -; Genomic_DNA.
DR EMBL; AOHS01000039; ELY29008.1; -; Genomic_DNA.
DR RefSeq; WP_004215694.1; NZ_AOHS01000039.1.
DR AlphaFoldDB; D3SUL2; -.
DR STRING; 547559.Nmag_1694; -.
DR PaxDb; 547559-Nmag_1694; -.
DR GeneID; 8824534; -.
DR KEGG; nmg:Nmag_1694; -.
DR PATRIC; fig|547559.17.peg.2349; -.
DR eggNOG; arCOG01887; Archaea.
DR HOGENOM; CLU_032621_3_1_2; -.
DR OrthoDB; 371821at2157; -.
DR Proteomes; UP000001879; Chromosome.
DR Proteomes; UP000011543; 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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001879}.
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 532..563
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 122..130
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT MOTIF 429..433
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT COMPBIAS 458..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 63965 MW; F086E5F92EEC2D07 CRC64;
MTGDDPREER GPEFEFEFDS DSDSDLEDEG EGKDKRAGLR TDGGAAGADD VALDPWGSST
VSDYRKLFEE FGIEEFDDVL PEVPHPHYLM RRGVIFGQRD YRPVVEALQN DEPAAVLSGF
MPTGDPHIGH KLVFDEIIWH QQQGADAYAL IADLEANSAR GMSWEEIDEH ARSYLLSLLA
LGFDPEEGDL YRQSTNREVQ DLAFDLGAEA NFSEFQAIYG FDGETDVSHM QSVVTQMADI
LYPQLEEPKP TVIPVGPDQD PHVRLARDLA ERMRFFKVST AYASFELDDG ERDLVARFHE
ELDPADFDDD QLRCVHVAQT LEATPLSELE VDASTLDGVL TKLNEAGMEP LRPRIRFSDR
RATEDAFDAL IDAIDGEKRV YENHIDAFEI DRADAAELAR EIEVDNGGYG FQPPSSIYHR
FMTGLTGGKM SSSVPASHIS LLDDPEDGYN KVKSATTGGR ETAEEQREKG GKADECPVYE
LYAYLLASDV HENEDRSRAA HQNPKDSEDD DEFAKRVYDE CVGGERLCGD CKEQAAQLMK
EFLAEHQEKR AEVEELLEKA DIELESPRRR
//
