ID A0A0G1JUW0_9BACT Unreviewed; 1345 AA.
AC A0A0G1JUW0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=UW37_C0004G0023 {ECO:0000313|EMBL:KKT47732.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_44_17.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618444 {ECO:0000313|EMBL:KKT47732.1, ECO:0000313|Proteomes:UP000034063};
RN [1] {ECO:0000313|EMBL:KKT47732.1, ECO:0000313|Proteomes:UP000034063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000256|ARBA:ARBA00001766};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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:KKT47732.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCIB01000004; KKT47732.1; -; Genomic_DNA.
DR PATRIC; fig|1618444.3.peg.123; -.
DR Proteomes; UP000034063; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKT47732.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 634..657
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 725..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 786..802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 823..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 954..971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1318..1341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..89
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 532..632
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 121..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..80
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1345 AA; 153072 MW; 8FC0DA9451AAD70D CRC64;
MKQEIKKILT EALADMGVVD LDPVVEISDM PGHGDYTTNV AMHLTKILRK SPMAIAEEIV
EQLEKDNRTK KGEIERIEAV KPGFINFFLS DEILITHPNL NNKIIRSRIK SGMTETLGMT
EKKSGNENAT DEAIRSKRDP SPLAGGLGMT KKKKRVMIEY TDPNPFKELH VGHLYSNAVG
ESLARLLTYT GNEVKRSDYF GDVGMHVAKS LWGLLKKMSD EKTSLSNLAE LSLVDRIHYL
GQAYAVGAAA YDDTTEKGKR VQEEMKDINY LIYVSAQEYM KKQFGWHPQV DYAKYITTSA
YSLPEIAKLY QTGRGWSMEY FESVFKRLGT TFDYYYPESI AGEYGAQIVK KYVGSVFEKS
EGAIVFRGEK YGLHTRVFIN SLGLPTYEAK ELGLAIAKHK DFKFDLCVNV TGNEIDEYFR
VVLTALQKVE PELAAKIKHI GHGMVRLPEG KMSSRTGNVM TGEWLIEEVK NKIYQILNTS
KLISQDLDKD DVAEKETIAA IKYSFLKVAL PSDITFDLDK SVSFEGDSGP YLLYAYARCR
SVMGKWTMDN GQWTMDNGKQ KRENTEERNL SRILFFFPEI VEDAGEHFAP NTLCSYLFSL
AQTFNLLYAK HEILGNTIFW ELRQWNACDG YMKLFLRLLP ILILTALVTG FFLPLFFPVP
QIFISPDSTL SDILHFFYPT KFLLSESLKE NKLPLWTDLV GTGFPLIAES QINALSFINL
VLFKFFPLIT AFNLQYVIIF LGLSIGMYVV AREFGWSKRT GLYCAIIYAF SGLHIVKIPH
LNCLQALSYV PFIFWIILRM QKNKQSKLWL VLPILLSQQI LQGHYQYVFM TYLFLGVYFY
LSWWRNQKKD HPWLMKKILT IGLMSVGLSM AQLVPSLEYF LKSGGRVGLG DTAIGSFHVH
HLLQFFYPYA LGDNRVGTYP APAYGLAFLE TFSYIGLIPL LLSLASVWFL KKDIWIRNCW
IIVALFFLFV FEKNSPMYVL FLVPPFSWFR VHSRFLAFIT FILVLLSGYV FERIGRKCFD
TFFVLFLFLV SIFDVISFAS SYQPMLPVSR VETIPDSLKL YTHHSRMAAV PYNTFSWSGR
MYTNGWKNPQ DYLYLVNEGK PNYTILSKIP NLSIYAGYLP LKQMKMLSTA LTTSERDEKE
KTATLSAATI TTLRLQNTGF LISPYTLSNP ELTFVTRIQT KNSQLDPFNL YELSDVKPPY
YLTDTYKTIR FVEQYDEEVQ KPGALTSYDA FLTTGRTLVS SGNQGTFAVV SDAATQKIFS
VSAPTDMFFV ASVYLYPGWE AVLDNTKTPL VPANLSGMAV FISKGKHTLM LQFIPKSLYL
GIGISIVTAV LYGVVIIRSV LKISS
//
