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Database: UniProt
Entry: I7C5B5_MYCHA
LinkDB: I7C5B5_MYCHA
Original site: I7C5B5_MYCHA 
ID   I7C5B5_MYCHA            Unreviewed;       427 AA.
AC   I7C5B5;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   ECO:0000313|EMBL:AFO51702.1};
GN   OrderedLocusNames=MHLP_00610 {ECO:0000313|EMBL:AFO51702.1};
OS   Mycoplasma haematolamae (strain Purdue).
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1212765 {ECO:0000313|EMBL:AFO51702.1, ECO:0000313|Proteomes:UP000006502};
RN   [1] {ECO:0000313|EMBL:AFO51702.1, ECO:0000313|Proteomes:UP000006502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Purdue {ECO:0000313|EMBL:AFO51702.1,
RC   ECO:0000313|Proteomes:UP000006502};
RX   PubMed=23105057; DOI=10.1128/JB.01557-12;
RA   Guimaraes A.M., Toth B., Santos A.P., do Nascimento N.C., Kritchevsky J.E.,
RA   Messick J.B.;
RT   "Genome Sequence of "Candidatus Mycoplasma haemolamae" Strain Purdue, a Red
RT   Blood Cell Pathogen of Alpacas (Vicugna pacos) and Llamas (Lama glama).";
RL   J. Bacteriol. 194:6312-6313(2012).
RN   [2] {ECO:0000313|Proteomes:UP000006502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Purdue {ECO:0000313|Proteomes:UP000006502};
RA   Guimaraes A.M.S., Toth B., Santos A.P., Nascimento N.C., Sojka J.E.,
RA   Messick J.B.;
RT   "Complete genome sequence of 'Candidatus Mycoplasma haemolamae'.";
RL   Submitted (JUL-2012) 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|HAMAP-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; CP003731; AFO51702.1; -; Genomic_DNA.
DR   AlphaFoldDB; I7C5B5; -.
DR   STRING; 1212765.MHLP_00610; -.
DR   KEGG; mhl:MHLP_00610; -.
DR   PATRIC; fig|1212765.3.peg.146; -.
DR   HOGENOM; CLU_025113_1_1_14; -.
DR   OrthoDB; 9800814at2; -.
DR   Proteomes; UP000006502; Chromosome.
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   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; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR015807; His-tRNA-ligase.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   NCBIfam; TIGR00442; hisS; 1.
DR   PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 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|HAMAP-Rule:MF_00127};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00127, ECO:0000313|EMBL:AFO51702.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006502}.
FT   DOMAIN          22..325
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   427 AA;  50334 MW;  FF5C2FF395A832D2 CRC64;
     MFAQPRGTRT VLGLELEKKN CLRRLLTELV KKSCFIEIET PMFEYKTLFT NDKDDPSNIL
     DKELFYLEGK KYALRPEGTA PVARAVVTEK LLHTLPSPLK FFYFAQCFRY ERPQKGRFRE
     FTQFGLEIIN ASSFIYEVET VKMIDSFLRN DLKLEKVELR INYLSSSETK AKWSKALTKY
     FLPLAEELSK TSQERIKVNP IRILDDRRDS QLKIVKAAPK ISDFLSKAEE EEIKEIRGLL
     NKLEIRYLWD PNLVRGLDYY TGLVFEWSLN NLAIAGGGRY DELFNRFCKR HQKEVDKVPS
     LGLAIGIDRL QEALNEAKFR WPILPEKKIY LCNLTNEVDP KIMKLIERLR EYEIVVDSNW
     DLQDLKSHFK YSSRLGIDWL LIYGPQERES REIILKQQFK NYKITFSLEN QEALIREIRD
     VLGREIP
//
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