ID   SYHM_DICDI              Reviewed;         501 AA.
AC   Q55D12;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Probable histidine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
DE   Flags: Precursor;
GN   Name=mhisS; ORFNames=DDB_G0269822;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72261.1; -; Genomic_DNA.
DR   RefSeq; XP_646319.1; XM_641227.1.
DR   AlphaFoldDB; Q55D12; -.
DR   SMR; Q55D12; -.
DR   STRING; 44689.DDB0231331; -.
DR   PaxDb; Q55D12; -.
DR   EnsemblProtists; EAL72261; EAL72261; DDB_G0269822.
DR   GeneID; 8617274; -.
DR   KEGG; ddi:DDB_G0269822; -.
DR   dictyBase; DDB_G0269822; mhisS.
DR   eggNOG; KOG1936; Eukaryota.
DR   HOGENOM; CLU_025113_1_0_1; -.
DR   InParanoid; Q55D12; -.
DR   OMA; MREFFQC; -.
DR   PhylomeDB; Q55D12; -.
DR   PRO; PR:Q55D12; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; ISS:dictyBase.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; ISS:dictyBase.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 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   PANTHER; PTHR43707; PTHR43707; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..501
FT                   /note="Probable histidine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000341689"
FT   REGION          32..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  57408 MW;  E55679117748674E CRC64;
     MLKTSNLISS LLHNNLKNTS ILRNKSIFYY STNSNNNNNN NNNNNNNNNN NKNINLQNIK
     GTYDLFPNEQ RIHKFIFDVG RGVAERYGFK EISTPIIEPF ELFNRSVGES SDIVMKEMFK
     FKDYSNESSS PPSMICLRPE GTAGVIRAII NQSSTNHLTP AQRYYYQGPM FRYERPQRGR
     QRQFHQLGVE LIGDQHPRSD VEIIDMAMNF IERLGINKSD TLLKINSLGD TDSIKVYNET
     LKRFYNDNVN KLSPISIKRL ERGNSLRILD SKERQDIELN KLAPSIQDSL SIQCKDRFNN
     VLKGLDCLGI SYEIDKSLVR GLDYYRHTIF EIQIIDNNQN NKGQRQQQQQ QQGLAILGGG
     RYDGLANQLG YKYKEILPSI GWASGIERMV LFLDQSKIPN SIRPIGIAIT DSSLSENAFK
     LCSNLRRNGW SSTLSTFNLE DENLSKQLKK FKNNPSFVII LAPSEYSNNT VIIKNMDDTT
     QSIIPLNEID NFLENNKVLK N