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Database: UniProt
Entry: A0A0L0CNE4_LUCCU
LinkDB: A0A0L0CNE4_LUCCU
Original site: A0A0L0CNE4_LUCCU 
ID   A0A0L0CNE4_LUCCU        Unreviewed;       499 AA.
AC   A0A0L0CNE4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=serine--tRNA ligase {ECO:0000256|ARBA:ARBA00012840};
DE            EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE   AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
GN   ORFNames=FF38_08987 {ECO:0000313|EMBL:KNC33840.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC33840.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC33840.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC33840.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC33840.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC         Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001032};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC         Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001706};
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-1 seryl-tRNA synthetase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010728}.
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:KNC33840.1}.
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DR   EMBL; JRES01000145; KNC33840.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0CNE4; -.
DR   STRING; 7375.A0A0L0CNE4; -.
DR   EnsemblMetazoa; KNC33840; KNC33840; FF38_08987.
DR   OMA; GYTPCFR; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00770; SerRS_core; 1.
DR   Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 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; IPR002317; Ser-tRNA-ligase_type_1.
DR   InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR   InterPro; IPR042103; SerRS_1_N_sf.
DR   InterPro; IPR033729; SerRS_core.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   NCBIfam; TIGR00414; serS; 1.
DR   PANTHER; PTHR11778:SF7; SERINE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11778; SERYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02403; Seryl_tRNA_N; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 2.
DR   PRINTS; PR00981; TRNASYNTHSER.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 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   Reference proteome {ECO:0000313|Proteomes:UP000037069}.
FT   DOMAIN          204..454
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   499 AA;  56122 MW;  D861938B76BDED60 CRC64;
     MVLDLDLFRS DKGGNPDAIR KNQELRFKDV GLVETVISQD TEWRQRRHRA DNLNKVKNVC
     SKVIGEKMKK KEPQGDEAAE VPAEVQQELT ELNAEKLGAL TVNQIKKVRV LIDQAMVENE
     RLLGEAEQKR NTALREVGNH LHESVPVSND EEENKVERTY GDCTKKGKYS HVDLIVMIDG
     MNGEKGTVVS GGRGYFLTGA AVFLEQALIQ HALHLLYAKN YTPLYTPFFM RKEVMQEVAQ
     LSQFDEELYK VVGKGSEKAE EGGVDEKYLI ATSEQPIAAY HRDEWLPEAS LPIKYAGLST
     CFRQEVGSHG RDTRGIFRVH QFEKIEQFVL TSPHDNKSWE MMDEMINNAE TFCQSLEIPY
     RIVNIVSGAL NHAASKKLDL EAWFAGSAAF RELVSCSNCL DYQARRLLVR YGQTKKMNAA
     VDYVHMLNAT MCATTRVICA ILETHQTETG VKVPEPLKKY MPEKFRDEIP FVKPAPIDVE
     AAAAANAKKP GKGKKDAAA
//
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