ID I3YQ01_ALIFI Unreviewed; 593 AA.
AC I3YQ01;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=Alfi_2815 {ECO:0000313|EMBL:AFL79069.1};
OS Alistipes finegoldii (strain DSM 17242 / JCM 16770 / CCUG 46020 / CIP
OS 107999 / KCTC 15236 / AHN 2437).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=679935 {ECO:0000313|EMBL:AFL79069.1, ECO:0000313|Proteomes:UP000006052};
RN [1] {ECO:0000313|Proteomes:UP000006052}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 17242 / JCM 16770 / AHN 2437 / CCUG 46020 / CIP 107999
RC {ECO:0000313|Proteomes:UP000006052};
RX PubMed=23961309; DOI=10.4056/sigs.3527032;
RA Mavromatis K., Stackebrandt E., Munk C., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Rohde M., Gronow S., Goker M.,
RA Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the bile-resistant pigment-producing anaerobe
RT Alistipes finegoldii type strain (AHN2437(T)).";
RL Stand. Genomic Sci. 8:26-36(2013).
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 -!- SUBUNIT: Monomer. {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; CP003274; AFL79069.1; -; Genomic_DNA.
DR RefSeq; WP_009598030.1; NC_018011.1.
DR AlphaFoldDB; I3YQ01; -.
DR STRING; 679935.Alfi_2815; -.
DR KEGG; afd:Alfi_2815; -.
DR PATRIC; fig|679935.3.peg.2729; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_10; -.
DR Proteomes; UP000006052; 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 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; IPR001412; aa-tRNA-synth_I_CS.
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 NCBIfam; TIGR00456; argS; 1.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}.
FT DOMAIN 1..87
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 476..593
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 122..132
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 593 AA; 66871 MW; 5379DBC824AFB872 CRC64;
MNIENFISDA VRRSVEALYG PLDGEQLQIQ KTRREFEGDY TLVTFPLLRR SRKSPEATAT
EIGEYMTANV PEVKSFNVIK GFLNLTLDCA FWAARFAEIA ADANFGQAPD TGRTVMIEYS
SPNTNKPLHL GHIRNNLLGY SVAQILRANG HNVIKANLVN DRGIHICKSM LAWKLYGNGE
TPASSGMKGD HLVGKYYVEF DKHYKAQIKE LTAQGQTEEE AKKNAPVMLE AQEMLRKWEA
KDPEVYSLWE TMNGWVYEGF DVTYKALGVD FDKIYYESQT YLLGKSLVEE GLRKGVFYRR
DDNSVWIDLT ADGLDEKLLL RGDGTSVYMT QDLGTAYRRF EENRLDDMIY VVGNEQNYHF
QVLKLILKKL GYADWSDHIT HLSYGMVELP EGKMKSREGT VVDADDLIAD MVSTAREMSD
ELGKLDGCTE EEADAVSTMV GLGALKYFIL KVDPKKTMLF DPRESIDFNG NTGPFIQYTH
ARICSVLRKA AEAGIDFSGA AQADYLPEEI ALVKSLTEYP SVVAAAGENF APSIVGAYVY
ELAKQFNGYY HDHSILKEEN DETRRMRLQL AQQVARVIRS GMKLLGIDVP ERM
//
