ID Q2HDT2_CHAGB Unreviewed; 517 AA.
AC Q2HDT2;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=histidine--tRNA ligase {ECO:0000256|ARBA:ARBA00012815};
DE EC=6.1.1.21 {ECO:0000256|ARBA:ARBA00012815};
GN ORFNames=CHGG_01622 {ECO:0000313|EMBL:EAQ93387.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ93387.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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}.
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DR EMBL; CH408029; EAQ93387.1; -; Genomic_DNA.
DR RefSeq; XP_001220843.1; XM_001220842.1.
DR AlphaFoldDB; Q2HDT2; -.
DR STRING; 306901.Q2HDT2; -.
DR GeneID; 4387092; -.
DR VEuPathDB; FungiDB:CHGG_01622; -.
DR eggNOG; KOG1936; Eukaryota.
DR HOGENOM; CLU_025113_4_1_1; -.
DR InParanoid; Q2HDT2; -.
DR OMA; CGGGNFK; -.
DR OrthoDB; 5476704at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
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; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR033656; HisRS_anticodon.
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.
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:UP000001056}.
FT DOMAIN 15..287
FT /note="Class II Histidinyl-tRNA synthetase (HisRS)-like
FT catalytic core"
FT /evidence="ECO:0000259|Pfam:PF13393"
FT DOMAIN 377..477
FT /note="Anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF03129"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 57132 MW; 6B15814B28820939 CRC64;
MAPKAPKFEI KTPKGTRDWS GPDMVLREKI FKTITDVFKR HGGITIDTPV FELKGKYGED
SKLIYDLADQ GGELCSLRYD LTVPFARYLA MNKDVTQIKR YHIAKVYRRD QPAVKKGRMR
EFGVYDAMIP DAEIIRIINE VFEGLGWQGK YTIKLNSRKI LDGLFQVCGV PDNLIRPISS
AVDKLDKMPW ADVKKEMVDE KGLAPEVADK IGKYVVLKGQ RDLIEKLKQD EDLAANPSMQ
QGFADMDLLF TYLEAFSAAH SVSFDLSLAR GLDYYTGVIY EVVTEGSAPT APASGDAKDK
PSKKKGGKPG DPDEDRSDDP TLGIGSIAAG GRYDNLVGMF SGKTQVPCVG ISFGIDRIFS
ITQASQKKKE RRNEVDVFVM AFGGGKDFSG LLTERSQICA RLWDAGIKAE FLYKVKPKLQ
NQFKAAETGG VPFALILGED ELAQGKAKLK EMGLPEDHPL KEGELISLDN LIEEVQTRLT
RKQELDSIVQ QAEGLKVVDG VKGEEVKAAA ETAQTAQ
//
