ID A0A1I5CFX0_PARPN Unreviewed; 494 AA.
AC A0A1I5CFX0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Histidine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00127};
DE EC=6.1.1.21 {ECO:0000256|HAMAP-Rule:MF_00127};
DE AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127};
DE Short=HisRS {ECO:0000256|HAMAP-Rule:MF_00127};
GN Name=hisS {ECO:0000256|HAMAP-Rule:MF_00127};
GN ORFNames=BDE18_2900 {ECO:0000313|EMBL:RKS44070.1}, HYQ43_06830
GN {ECO:0000313|EMBL:QLH13958.1};
OS Paracoccus pantotrophus (Thiosphaera pantotropha).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=82367 {ECO:0000313|EMBL:QLH13958.1, ECO:0000313|Proteomes:UP000509322};
RN [1] {ECO:0000313|EMBL:RKS44070.1, ECO:0000313|Proteomes:UP000273626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 /
RC NCCB 82005 / GB17 {ECO:0000313|Proteomes:UP000273626}, and DSM 2944
RC {ECO:0000313|EMBL:RKS44070.1};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QLH13958.1, ECO:0000313|Proteomes:UP000509322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC10489 {ECO:0000313|EMBL:QLH13958.1,
RC ECO:0000313|Proteomes:UP000509322};
RA Si Y.;
RT "The complete genome of Paracoccus pantotrophus ACCC 10489.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001137, ECO:0000256|HAMAP-
CC Rule:MF_00127};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00127}.
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DR EMBL; CP058689; QLH13958.1; -; Genomic_DNA.
DR EMBL; RBLI01000002; RKS44070.1; -; Genomic_DNA.
DR RefSeq; WP_028709866.1; NZ_RIAQ01000018.1.
DR AlphaFoldDB; A0A1I5CFX0; -.
DR GeneID; 51370084; -.
DR OrthoDB; 9800814at2; -.
DR Proteomes; UP000273626; Unassembled WGS sequence.
DR Proteomes; UP000509322; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_00127; His_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR033656; HisRS_anticodon.
DR NCBIfam; TIGR00442; hisS; 1.
DR PANTHER; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11476; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00127};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00127};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00127};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00127};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00127};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00127}.
FT DOMAIN 1..383
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 52832 MW; 95B2CBA085689C83 CRC64;
MAKDQKKQPR PKAETPKGFR DYFGADVTER KQMLDRIAEI YHRHGFEPLE TSAVETVEAL
GKFLPDVDRP NAGVFAWQES DVPGGGSGDW LALRYDLTAP LARVAAQFRN DLPSPYRRYA
MGPVWRNEKP GPGRFRQFYQ CDADTVGSAS VAADAEICAM LAAALEHAGI ARGDYLIRIN
NRKVLNGILE STGVAEGKPA DDVLRTIDKF DKVGEEGVRQ LLTTGRKDDS GAFIEGVGLA
PEQAGPVLAF LTSKGADNAA TLQNLRAAVG ASAAGAEGVA ELAQIAQMLA AMGVGEDRAV
IDPSIVRGLG YYTGPVFEAE LTFEILDDKG RKRQFGSVAG GGRYDGLVER FTGQKVPATG
VSIGVDRLLA ALRAKGLMGG AEPGPVVVTV MDRERMADYQ AMAAELRAAG IRAEVYLGNP
KNFGNQLKYA DKRNAPVAII QGGDEAARGV VQVKDLVLGA KIAAEASHEE WKAQPAQTEV
ARADLVAEVR RILG
//