ID Q9VQL1_DROME Unreviewed; 501 AA. AC Q9VQL1; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 04-NOV-2026, entry version 216. 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 Name=SerRS {ECO:0000313|EMBL:AAF51155.1, GN ECO:0000313|FlyBase:FBgn0031497}; GN Synonyms=Dmel\CG17259 {ECO:0000313|EMBL:AAF51155.1}, DmSRS1 GN {ECO:0000313|EMBL:AAF51155.1}; GN ORFNames=CG17259 {ECO:0000313|EMBL:AAF51155.1, GN ECO:0000313|FlyBase:FBgn0031497}, Dmel_CG17259 GN {ECO:0000313|EMBL:AAF51155.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AAF51155.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [9] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [10] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E., RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M., RA Gelbart W.M., null; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [11] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E., RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M., RA null; RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [12] {ECO:0000313|EMBL:AAF51155.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=25589440; RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E., RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M., RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M., RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M., RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M., RA Karpen G.H., Celniker S.E.; RT "The Release 6 reference sequence of the Drosophila melanogaster genome."; RL Genome Res. 25:445-458(2015). RN [13] {ECO:0000313|EMBL:AAF51155.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (DEC-2023) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|EMBL:AAF51155.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., RA Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (AUG-2025) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + CC diphosphate + H(+); 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:ARBA00047929}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + CC diphosphate + H(+); 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:ARBA00048823}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type-1 seryl-tRNA synthetase subfamily. CC {ECO:0000256|ARBA:ARBA00010728}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014134; AAF51155.1; -; Genomic_DNA. DR EMBL; AE014134; AGB92519.1; -; Genomic_DNA. DR RefSeq; NP_001259982.1; NM_001273053.1. DR RefSeq; NP_608743.2; NM_134899.3. DR AlphaFoldDB; Q9VQL1; -. DR SMR; Q9VQL1; -. DR IntAct; Q9VQL1; 141. DR STRING; 7227.FBpp0077351; -. DR PaxDb; 7227-FBpp0077351; -. DR PeptideAtlas; Q9VQL1; -. DR DNASU; 33518; -. DR GeneID; 33518; -. DR KEGG; dme:Dmel_CG17259; -. DR UCSC; CG17259-RA; d. melanogaster. DR AGR; FB:FBgn0031497; -. DR CTD; 33518; -. DR FlyBase; FBgn0031497; SerRS. DR VEuPathDB; VectorBase:FBgn0031497; -. DR eggNOG; KOG2509; Eukaryota. DR HOGENOM; CLU_023797_0_0_1; -. DR OMA; AACDQTM; -. DR OrthoDB; 10264585at2759; -. DR BioGRID-ORCS; 33518; 0 hits in 3 CRISPR screens. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0031497; Expressed in eye disc (Drosophila) and 123 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; TAS:FlyBase. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IDA:FlyBase. DR GO; GO:0004828; F:serine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IBA:GO_Central. DR CDD; cd00770; SerRS_core; 1. DR FunFam; 1.10.287.40:FF:000002; Serine--tRNA ligase, cytoplasmic; 1. DR FunFam; 3.30.930.10:FF:000027; Serine--tRNA ligase, cytoplasmic; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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; 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; 1. 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 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR001529- KW 2}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AAF51155.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9VQL1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 204..454 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT BINDING 272 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-1" FT BINDING 303..305 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-2" FT BINDING 303 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-1" FT BINDING 319..322 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-2" FT BINDING 326 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-1" FT BINDING 392..395 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-2" FT BINDING 428 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-1" FT SITE 430 FT /note="Important for serine binding" FT /evidence="ECO:0000256|PIRSR:PIRSR001529-1" SQ SEQUENCE 501 AA; 56456 MW; 877778B691FE666A CRC64; MVLDLDLFRS DKGGNPDLVR ENQKKRFKDV ALVETVIAKD TEWRQCRHRA DNLNKVKNVC SKVIGEKMKK KEPVGAMSED LPADVTKDLT EIVAETLQPL TVNQIKQLRV LIDDAMTENQ KSLELAEQTR NTSLREVGNH LHESVPVSND EDENRVERTF GDCEKRGKYS HVDLIVMIDG MNAEKGAVVS GGRGYFLTGA AVFLEQALIQ HALHLLYARD YVPLYTPFFM RKEVMQEVAQ LSQFDEELYK VVGKGSEKAE EVGIDEKYLI ATSEQPIAAY HRDEWLPESS LPIKYAGLST CFRQEVGSHG RDTRGIFRVH QFEKVEQFVL TSPHDNKSWE MMDEMIGNAE QFCQSLGIPY RVVNIVSGAL NHAASKKLDL EAWFGGSGAY RELVSCSNCL DYQARRLLVR FGQTKKMNAA VDYVHMLNAT MCAATRVICA ILETHQTETG IKVPEPLKKY MPAKFQDEIP FVKPAPIDLE LAAAEKQKGK KEKTKKDPAA G //