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Database: UniProt
Entry: Q4N6F8_THEPA
LinkDB: Q4N6F8_THEPA
Original site: Q4N6F8_THEPA 
ID   Q4N6F8_THEPA            Unreviewed;       563 AA.
AC   Q4N6F8;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Methionyl-tRNA synthetase, putative {ECO:0000313|EMBL:EAN34450.1};
GN   OrderedLocusNames=TP01_1212 {ECO:0000313|EMBL:EAN34450.1};
OS   Theileria parva (East coast fever infection agent).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5875 {ECO:0000313|EMBL:EAN34450.1, ECO:0000313|Proteomes:UP000001949};
RN   [1] {ECO:0000313|EMBL:EAN34450.1, ECO:0000313|Proteomes:UP000001949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Muguga {ECO:0000313|EMBL:EAN34450.1,
RC   ECO:0000313|Proteomes:UP000001949};
RX   PubMed=15994558; DOI=10.1126/science.1110439;
RA   Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA   Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA   Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA   Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA   Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA   Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA   Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA   Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT   "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT   lymphocytes.";
RL   Science 309:134-137(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
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:EAN34450.1}.
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DR   EMBL; AAGK01000001; EAN34450.1; -; Genomic_DNA.
DR   RefSeq; XP_766733.1; XM_761640.1.
DR   AlphaFoldDB; Q4N6F8; -.
DR   STRING; 5875.Q4N6F8; -.
DR   EnsemblProtists; EAN34450; EAN34450; TP01_1212.
DR   GeneID; 3502387; -.
DR   KEGG; tpv:TP01_1212; -.
DR   VEuPathDB; PiroplasmaDB:TpMuguga_01g01212; -.
DR   eggNOG; KOG0436; Eukaryota.
DR   InParanoid; Q4N6F8; -.
DR   OMA; MDTQAFC; -.
DR   Proteomes; UP000001949; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001949};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          86..202
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   DOMAIN          207..423
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          441..526
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   563 AA;  64658 MW;  F382E5D30AF412B2 CRC64;
     MQILFNNANG SVNFTKILFF HLIILNFSLS FRIPNTFKRD SSFLTHHSLN PRLNDKFSVN
     LFSDPGVSSG NKYLITTPLF YLNGPPHLGH AYTLVSSDVL KRFLILSGHD CKLLAGTDEH
     GSKIKTTAAN FGYSPKEYVI SMRNQFFKLY KAYDITPEIV VHTSENEHKS KVKRVFDNFL
     ESGHIYRGLH RGYFSPKEDL YYTESKLING KSPLGFDVTL VDEPAYFFKL DIWKRKLVEF
     FKDSEVILPQ HSLNEVRKLL QSEINDIAIT RSNCDWGIPI TNSGNETVYV WFDALLGYLT
     HLHSFPPLEQ SNSNLNGLKI IHVIGKDILT FHTILWPAIL MALKLDIKLR FLVHGWLLNK
     GEKISKSLNN SISPLNTSVP SDVSRFALMN LGDFSYDFEF DPSMFDNALK TLRNKFANTF
     YRVTSILQMN KVDTVQPCDC DHKLLEKFNK YSEEIRNSVQ SFRLDRYIQI LVEMSSEVNK
     FIELTQFWTM SSQSELLNTS WICCTLLLYI SIYLAPITPK LANDMILRLG PQLSGAPVKT
     ISFNLLDDIQ HISYNPKHLN PLI
//
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