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Database: UniProt
Entry: H9ZZI3_FERFK
LinkDB: H9ZZI3_FERFK
Original site: H9ZZI3_FERFK 
ID   H9ZZI3_FERFK            Unreviewed;       653 AA.
AC   H9ZZI3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE            EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE            Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN   Name=argS {ECO:0000256|HAMAP-Rule:MF_00123};
GN   OrderedLocusNames=FFONT_0148 {ECO:0000313|EMBL:AFH42140.1};
OS   Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC   Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC   Fervidicoccus.
OX   NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH42140.1, ECO:0000313|Proteomes:UP000007391};
RN   [1] {ECO:0000313|Proteomes:UP000007391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC   {ECO:0000313|Proteomes:UP000007391};
RA   Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA   Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Fervidicoccus fontis complete genome analysis confirms its distinct
RT   phylogenetic position and predicts its environmental function.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFH42140.1, ECO:0000313|Proteomes:UP000007391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC   {ECO:0000313|Proteomes:UP000007391};
RX   PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA   Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA   Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA   Ravin N.V.;
RT   "Analysis of the complete genome of Fervidococcus fontis confirms the
RT   distinct phylogenetic position of the order Fervidicoccales and suggests
RT   its environmental function.";
RL   Extremophiles 18:295-309(2014).
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         ECO:0000256|HAMAP-Rule:MF_00123};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC       ECO:0000256|RuleBase:RU363038}.
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DR   EMBL; CP003423; AFH42140.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9ZZI3; -.
DR   STRING; 1163730.FFONT_0148; -.
DR   KEGG; ffo:FFONT_0148; -.
DR   eggNOG; arCOG00487; Archaea.
DR   HOGENOM; CLU_006406_6_1_2; -.
DR   InParanoid; H9ZZI3; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 372102at2157; -.
DR   Proteomes; UP000007391; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR   InterPro; IPR001278; Arg-tRNA-ligase.
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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
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_00123};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00123}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00123};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00123}; Reference proteome {ECO:0000313|Proteomes:UP000007391}.
FT   DOMAIN          537..653
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   MOTIF           136..146
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ   SEQUENCE   653 AA;  75222 MW;  39384ADE2B0F5815 CRC64;
     MANLPLSIND KYLYNRILLA LRESLDDELG PSSQDRLFLI SEPPENVDAD LSYPLVREIR
     QMKRGIEDYT KELSRKLTEA SGVKIDATYT SGYLNLKFNR VEFAKKFFEE FFRDLDNYGG
     GQAVKKLNIV VEHTSANPLH PLHIGHARNS CLGDTISRLL KFYGMNIERR FYIDDMGRQM
     ALLIYGILKL NEDGDWKRFL NEEKIDHRIG EIYAATNILV EINELKKKIK SASEDDYQAL
     IAQQDELVAE SARIRDRSPE IFDVLAEKIM KDEDPEKEIS QLSLRYEQHD ENVVKIFREV
     IELVIGGFKE TLGKLGIEFD KWDYESDLVW SGLVDEILRK ARESQVFTIY KGAEALSYET
     ILNDSLKEKL FIPKEMDIPP LILKRSDGTT LYTTRDIAYS IKKFKEFNAD YVINVIAKEQ
     TLPQAQLRLA LYSLGYREYA ERLIHYSYEM VNLPGYKMSG RRGRFVSLDE LIEMSENAAK
     QELLKRKGQV AEDVEQVYKA VGRSAVRYSL VSISSEKPLV LKLNDVINFE KNTAPYVQYT
     YARAFSLLAK AGSYERPTEF DIIEKDDQTY KLIRSLSKFP WVIHKSTTEL KPELIVAYLG
     DISQKFNSWY DNVPVLGEKD ERYRALKIAT VNAVKSIIGS ALNIVGVVTL EKM
//
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