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Database: UniProt
Entry: J8PGS7_SACAR
LinkDB: J8PGS7_SACAR
Original site: J8PGS7_SACAR 
ID   J8PGS7_SACAR            Unreviewed;       544 AA.
AC   J8PGS7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE            EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
GN   ORFNames=SU7_3641 {ECO:0000313|EMBL:EJS41330.1};
OS   Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS41330.1, ECO:0000313|Proteomes:UP000006968};
RN   [1] {ECO:0000313|EMBL:EJS41330.1, ECO:0000313|Proteomes:UP000006968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-6 / AS 2.3317 / CBS 10644
RC   {ECO:0000313|Proteomes:UP000006968};
RX   PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA   Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA   Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA   Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT   "High quality de novo sequencing and assembly of the Saccharomyces
RT   arboricolus genome.";
RL   BMC Genomics 14:69-69(2013).
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};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJS41330.1}.
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DR   EMBL; ALIE01000195; EJS41330.1; -; Genomic_DNA.
DR   AlphaFoldDB; J8PGS7; -.
DR   HOGENOM; CLU_025113_4_0_1; -.
DR   OrthoDB; 5476704at2759; -.
DR   Proteomes; UP000006968; Chromosome XVI.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   CDD; cd00859; HisRS_anticodon; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006968}.
FT   DOMAIN          69..421
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   REGION          21..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  60297 MW;  E0E085A46EF6D0F8 CRC64;
     MFSRTINRVV SSIKSSSITR MSSATSSAPA APKAPKAPKA PKASKKNKLQ VSLKTPKGTK
     DWADTDMIIR EAIFNTLSNL FKKHGGVTID TPVFELREIL AGKYGEDSKL IYNLEDQGGE
     LCSLRYDLTV PFARYVAMNN IQNIKRYHIA KVYRRDQPAM TKGRMREFYQ CDFDVAGSYE
     SMVPDAECLS ILVEGITSLG IRDFKIKLNH RKILDGIFQI SGVKDEDVRK ISSAVDKLDK
     SPWEAVKKEM TEEKGQSEET ADKIGEYVKL NGSLKEIHTV LSQDSTITSN ELAKQGLDEI
     ATLIKYTEAF NIDSFISFDL SLARGLDYYT GLIYEVVTSA SAPPKNASEL KKKAKSVEDA
     SEFVGVGSIA AGGRYDNLVN MFAEASGKKS TQIPCVGISF GVERLFSLIK QRIDSSTFIK
     PTATQVFVMA FGGGKDWTGY LAERMKVTKQ LWDAGIEAEY VYKSKANPRK QFDAAEKAGC
     HIAVILGKEE YLEGKLRVKR LGQEFANDDG ELVKATDIVA IVREKLSQIH EDGLNEVTRL
     IKGL
//
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