ID H2APX2_KAZAF Unreviewed; 729 AA.
AC H2APX2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=threonine--tRNA ligase {ECO:0000256|ARBA:ARBA00013163};
DE EC=6.1.1.3 {ECO:0000256|ARBA:ARBA00013163};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031900};
GN Name=KAFR0B01230 {ECO:0000313|EMBL:CCF56422.1};
GN ORFNames=KAFR_0B01230 {ECO:0000313|EMBL:CCF56422.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF56422.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF56422.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000070};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR EMBL; HE650822; CCF56422.1; -; Genomic_DNA.
DR RefSeq; XP_003955557.1; XM_003955508.1.
DR AlphaFoldDB; H2APX2; -.
DR STRING; 1071382.H2APX2; -.
DR GeneID; 13882646; -.
DR KEGG; kaf:KAFR_0B01230; -.
DR eggNOG; KOG1637; Eukaryota.
DR HOGENOM; CLU_008554_0_1_1; -.
DR InParanoid; H2APX2; -.
DR OrthoDB; 1119631at2759; -.
DR Proteomes; UP000005220; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd01667; TGS_ThrRS; 1.
DR CDD; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR047246; ThrRS_anticodon.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF46; THREONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220}.
FT DOMAIN 65..127
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 308..617
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 84631 MW; 2FA923B429D8AC96 CRC64;
MSAAAEVTEQ VKKMSVDDKK PKVQKKSKQQ MLYMDPEPQF IQERIEFFEK LQREYHEKIS
SLGRNPIKIV LKDGSIKVGT SWETTPLDIA REISKSLADR LCIAKVNGQL WDLERPFEGE
SNEELKLELL DFESDEGKRV FWHSSAHVLG EACECNLGAH ICLGPPTDDG FFYEFATRDS
LRDPSECEER TVSQADFPNL EGVAKDVIKQ KQKFERLVMS KEDLLKMFHY SKYKTYLVQT
KIPDGGATTV YRCGKLIDLC VGPHIPHTGR IKAFKLLKNS SCYFLGDAEN DSLQRVYGVS
FPDKKLMDAH LKFLEEAQKR DHRKLGREQE LFMFNEMSPG SAFWLPHGTR IYNTLVDLLR
GEYRKRGYEE VITPNMYNSK LWETSGHWAN YKENMFSFEV EKETYGLKPM NCPGHCLMFK
SRERSYRELP WRVADFGVIH RNEFSGALSG LTRVRRFQQD DAHIFCTQDQ IESEIENIFD
FLKFVYGVFG FEFKMELSTR PEKYVGELET WNAAEKKLES ALNKWGGNWE LNPGDGAFYG
PKIDIMISDA LRRWHQCATI QLDFQLPNRF ELEFKAKDNK EEANENYERP VMIHRAILGS
VERMTAILTE HFAGKWPFWL SPRQVLVVPV GVKYQDYAQE VRDQLHDAGF YADVDLSGNT
LQKKVRNGQL LKYNFIFIVG EQEMTEKSVN IRNRDVMEQQ GKNATISLAT VIEQLNNLKE
EKRNDNMLN
//
